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Journal articles on the topic 'Polyclonal antiserum AS'

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Published: 4 June 2021

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Köves, K., and A. Arimura. "Solid-phase adsorption method for removing undesired antibodies from polyclonal antiserum." Journal of Histochemistry & Cytochemistry 37, no. 6 (1989): 903–8. http://dx.doi.org/10.1177/37.6.2723405.

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We have developed a novel and simple method, requiring only a small amount of antigen, for removal of undesired antibodies from antiserum. The method was established using a well-characterized antiserum against rat luteinizing hormone (anti-rLH). Wells of polystyrene tissue culture plates were coated with rat LH (rLH). Anti-rLH diluted 1:3000 was added to rLH-coated wells and shaken to remove LH antibodies. Control anti-rLH was treated in a similar manner in non-rLH-coated wells. Both antisera were tested by immunocytochemistry on rat pituitaries. Antiserum from rLH-coated wells stained no cells, whereas the control serum stained cells that were morphologically typical of LH cells. The effectiveness of this antibody removal was also confirmed in a modified ELISA. In another experiment, anti-rLH and anti-hTSH beta sera were mixed. The final dilution of both antisera was 1:10,000. Anti-rLH was removed by the purification method described. Completeness of antibody removal was confirmed by a double-immunohistochemical staining of rat pituitary in which sections were first stained by the PAP method and then stained with an immunofluorescence procedure after elution of the first antigen-antibody complex. The mixed antiserum incubated in rLH-coated wells did not stain LH cells. There was no co-localization between the LH immunopositivity demonstrated by an anti-rLH serum using immunofluorescence and cells immunostained with the purified antiserum using the PAP method. As indicated in ELISA, the titer of the TSH beta antiserum was not decreased compared to that of the untreated, mixed control antiserum, and the LH antibodies were eliminated by the treatment. This new purification method has four distinct advantages: (a) antiserum is not treated chemically; (b) it requires only a small amount of antigen compared with the amount required for affinity chromatography; (c) neither the undesired antigen-antibody complex(es) nor an excess amount of antigen is present in the purified antiserum; and (d) removal of undesired antibodies can be monitored by ELISA.

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Hoving, H. J. T., J. D. Venter, D. E. Worst, and M. R. Lipinski. "Adaptation of an immunodot assay for multiple prey identification of squid paralarvae in field trials." Journal of the Marine Biological Association of the United Kingdom 85, no. 6 (2005): 1499–501. http://dx.doi.org/10.1017/s0025315405012695.

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An optimized method, using polyclonal antibodies in an immunoassay, for prey detection in the diet of paralarvae of South African Loligo reynaudii is described. The study has increased the specificity of the antisera by determining the optimum antiserum dilutions and the detection limits of the antisera. Unfed laboratory-hatched paralarvae (negative control) were exposed to antisera and showed cross-reactions with polychaete antiserum.

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Shahangian, S., K. A. Agee, and R. P. Dickinson. "Concentration Dependencies of Immunoturbidimetric Dose-Response Curves: Immunoturbidimetric Titer and Reactivity, and Relevance to Design of Turbidimetric Immunoassays." Clinical Chemistry 38, no. 6 (1992): 831–40. http://dx.doi.org/10.1093/clinchem/38.6.831.

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Abstract To characterize polyclonal antisera for two-point immunoturbidimetric applications, we defined, as functions of antiserum concentration, two parameters derived from dose-response curves: the maximum bichromatic optical response, Tmax, and the antigen concentration in the region of excess antibody corresponding to one-half Tmax, or C50. We raised monospecific polyclonal antisera in goats against several human immunoglobulins, C-reactive protein, C3, C4, apolipoproteins A-I and B, and several other proteins. We could linearly relate the logarithm of the antiserum concentration to log C50 and to log Tmax. The concentration of polyethylene glycol affected not only C50 and Tmax but also their functional dependencies on antiserum concentration. We devised two definitions of immunoturbidimetric titer and related them to the titer obtained by the single radial immunodiffusion method of Becker (Immunochemistry 1969; 6:539-46).

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Parry, R. A., C. B. McLean, M. R. Alderton, P. J. Coloe, and A. C. Lawrie. "Polyclonal antisera to epacrid mycorrhizae and to Hymenoscyphus ericae display specificity." Canadian Journal of Botany 78, no. 7 (2000): 841–50. http://dx.doi.org/10.1139/b00-052.

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Three polyclonal antisera produced in mice were used to investigate specificity and cross-reactivity between ericaceous and epacridaceous mycorrhizal fungi. One antiserum was to a culture of Hymenoscyphus ericae (Read) Korf and Kernan, the fungal endophyte of Calluna vulgaris (L.) Hull (Ericaceae). The other two were to peloton preparations from roots of Epacris impressa Labill. (Epacridaceae) from two sites (Cranbourne and Grampians) in Victoria, Australia. By immunofluorescence, all three antisera recognised H. ericae but not Oidiodendron griseum Roback, suggesting a serological relationship with the former endophyte. They also recognised 10 of the 12 fungal isolates tested, from mycorrhizal roots of E. impressa (Cranbourne), and all 4 isolates from Astroloma pinifolium (R. Br.) Benth. (Epacridaceae) (Grampians). Furthermore, none of the antisera recognised any of the nine common soil-inhabiting fungi selected for screening. Antisera recognised only unmelanized hyphae on epacrid and other plant roots taken from the wild. With plants from Cranbourne, all antisera except the Grampians antiserum recognised hyphae only on epacrid roots, demonstrating specificity. Hyphae on other plant roots were not recognised by any of the antisera. With plants from the Grampians, all antisera recognised some hyphae on both epacrid and other plant roots, except in two instances. The immunogold labelling indicates that the antisera are specific for fungi and do not recognise the plant. Since the fungal isolate forms true mycorrhizal structures, this suggests that there is a serological similarity between fungi forming epacrid mycorrhiza and those (H. ericae) forming ericoid mycorrhiza.Key words: ericoid mycorrhizae, Epacridaceae, polyclonal antibodies, immunofluorescence, immunogold.

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CLEVELAND, S. M., H. P. TAYLOR, and N. J. DIMMOCK. "Selection of neutralizing antibody escape mutants with type A influenza virus HA-specific polyclonal antisera: possible significance for antigenic drift." Epidemiology and Infection 118, no. 2 (1997): 149–54. http://dx.doi.org/10.1017/s0950268896007303.

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Ten antisera were produced in rabbits by two or three intravenous injections of inactivated whole influenza type A virions. All contained haemagglutination-inhibition (HI) antibody directed predominantly to an epitope in antigenic site B and, in addition, various amounts of antibodies to an epitope in site A and in site D. The ability of untreated antisera to select neutralization escape mutants was investigated by incubating virus possessing the homologous haemagglutinin with antiserum adjusted to contain anti-B epitope HI titres of 100, 1000 and 10000 HIU/ml. Virus-antiserum mixtures were inoculated into embryonated hen's eggs, and progeny virus examined without further selection. Forty percent of the antisera at a titre of 1000 HIU/ml selected neutralizing antibody escape mutants as defined by their lack of reactivity to Mab HC10 (site B), and unchanged reactivity to other Mabs to site A and site D epitopes. All escape mutant-selecting antisera had a ratio of anti-site B (HC10)-epitope antibody[ratio ]other antibodies of [ges ]2·0[ratio ]1. The antiserum with the highest ratio (7·4[ratio ]1) selected escape mutants in all eggs tested in four different experiments. No antiserum used at a titre of 10000 HIU/ml allowed multiplication of any virus. All antisera used at a titre of 100 HIU/ml permitted virus growth, but this was wild-type (wt) virus. We conclude that a predominant epitope-specific antibody response, a titre of [ges ]1000 HIU/ml, and a low absolute titre of other antibodies ([les ]500 HIU/ml) are three requirements for the selection of escape mutants. None of the antisera in this study could have selected escape mutants without an appropriate dilution factor, so the occurrence of an escape mutant-selecting antiserum in nature is likely to be a rare event.

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Michon, Francis, Samuel L. Moore, John Kim, et al. "Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera." Infection and Immunity 73, no. 10 (2005): 6383–89. http://dx.doi.org/10.1128/iai.73.10.6383-6389.2005.

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ABSTRACT A number of epitope specificities associated with the cell wall polysaccharide antigen of group A streptococci were identified in a polyclonal rabbit antiserum induced in rabbits by whole group A streptococci and in polyclonal convalescent human antisera from children that had recovered from streptococcal A infections. The identification was achieved by using a series of synthetic oligosaccharides, glycoconjugates, and bacterial polysaccharide inhibitors to inhibit the binding of the group A helical polysaccharide to the polyclonal antisera. The exclusively dominant epitope expressed in the convalescent human antisera was the doubly branched extended helical hexasaccharide with the structure α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap. The hexasaccharide epitope also bound with the highest immunoreactivity to the rabbit antiserum. In contrast, the human antisera did not show significant binding to the singly branched pentasaccharide with the structure α-l-Rhap(1→2)α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap or the branched trisaccharide α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap, although both these haptens bound significantly to the same rabbit antiserum, albeit with less immunoreactivity than the hexasaccharide. Inhibition studies using streptococcal group A and B rabbit antisera and the inhibitors indicated above also suggested that the group A carbohydrate, unlike the group B streptococcal polysaccharide, does not contain the disaccharide α-l-Rhap(1→2)α-l-Rhap motif at its nonreducing chain terminus, stressing the importance of mapping the determinant specificities of these two important streptococcal subcapsular group polysaccharides to fully understand the serological relationships between group A and group B streptococci.

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Wassef, Nabila M., Glenn M. Swartz Jr., Carl R. Alving, and Morris Kates. "Antibodies to liposomal phosphatidylcholine and phosphatidylsulfocholine." Biochemistry and Cell Biology 68, no. 1 (1990): 54–64. http://dx.doi.org/10.1139/o90-007.

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Antibodies against dimyristoyl phosphatidylsulfocholine or dimyristoyl phosphatidylcholine were raised in rabbits after injection of liposomes containing phosphatidylsulfocholine or phosphatidylcholine, cholesterol, and lipid A. The antibody activities were assayed by complement-dependent immune damage to liposomes and by a solid-phase, enzyme-linked immunosorbent assay using purified dimyristoyl phosphatidylcholine or dimyristoyl phosphatidylsulfocholine as antigen. Each antiserum raised against phosphatidylsulfocholine reacted with liposomes containing phosphatidylcholine, and each antiserum raised against phosphatidylcholine reacted with liposomes containing phosphatidylsulfocholine. However, adsorption of dimyristoyl phosphatidylsulfocholine antiserum with liposomes containing dimyristoyl phosphatidylcholine removed all activity against dimyristoyl phosphatidylcholine, but did not eliminate antibody activity against dimyristoyl phosphatidylsulfocholine. These results indicate that the antiserum against phosphatidylsulfocholine contained mixed populations of antibodies. Polyclonal antisera that have been appropriately adsorbed can therefore be obtained with a high degree of specificity for phosphatidylsulfocholine and such antisera can distinguish between phosphatidylsulfocholine and phosphatidylcholine.Key words: liposomes, antibodies, phosphatidylsulfocholine, phosphatidylcholine.

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Abouzid, A. M., J. Freitas-Astua, D. E. Purcifull, et al. "Serological Studies Using Polyclonal Antisera Prepared Against the Viral Coat Protein of Four Begomoviruses Expressed in Escherichia coli." Plant Disease 86, no. 10 (2002): 1109–14. http://dx.doi.org/10.1094/pdis.2002.86.10.1109.

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Polyclonal rabbit antisera were produced to the coat protein of Bean golden mosaic virus Brazil isolate (BGMV), Cabbage leaf curl virus (CabLCV), Tomato yellow leaf curl virus (TYLCV), and Tomato mottle virus (ToMoV), all expressed in Escherichia coli by the pETh expression vector. The expressed coat protein of each virus was purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis for use as an immunogen. The antisera to BGMV, CabLCV, TYLCV, and ToMoV reacted in indirect (plate-trapping) enzyme-linked immunosorbent assay (ELISA) with extracts from begomovirus-infected tissue. The antisera to BGMV, CabLCV, TYLCV, and ToMoV also reacted specifically with the test begomovirus antigens in leaf imprint blots and Western blots. The CabLCV and TYLCV antisera were used to detect Bean golden yellow mosaic virus antigens by immunogold labeling of thin sections of infected bean tissues. In tissue blot immunoassays, the TYLCV antiserum reacted well with TYLCV antigens but not with ToMoV antigens, while CabLCV antiserum reacted well with ToMoV antigens and weakly with TYLCV antigens. The results indicate that polyclonal antisera prepared to expressed begomovirus coat proteins were useful for the detection of begomoviruses in an array of assays.

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Banerji, Benoy, and Carl R. Alving. "Antibodies to liposomal phosphatidylserine and phosphatidic acid." Biochemistry and Cell Biology 68, no. 1 (1990): 96–101. http://dx.doi.org/10.1139/o90-012.

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Polyclonal antisera to phosphatidylserine or phosphatidic acid were induced in rabbits by injecting liposomes containing phosphatidylserine or phosphatidic acid and lipid A. Adsorption of antisera with liposomes containing different phospholipids revealed that some degree of reactivity with one or more phospholipids other than the immunizing phospholipid was often observed. However, cross-reactivity with other phospholipids was not a universal phenomenon, and one antiserum to phosphatidylserine failed to cross-react (i.e., was not adsorbed) with liposomes containing other phospholipids. All of the antisera were inhibited by soluble phosphorylated haptens (e.g., phosphocholine but not choline), but one of the antisera to phosphatidylserine was inhibited both by phosphoserine and by serine alone. Liposomal membrane composition influenced the activity of antiserum to phosphatidylserine. Regardless of whether unsaturated (beef brain) or saturated (dimyristoyl) phosphatidylserine was used in the immunizing liposomes, the antisera reacted more vigorously with liposomes containing unsaturated than saturated phosphatidylserine. We conclude that liposomes containing lipid A can serve as vehicles for stimulating polyclonal antisera to phosphatidylserine and phosphatidic acid. Although cross-reactivity with certain other phospholipids can be observed, sera from selected animals apparently can exhibit a high degree of specific activity to the immunizing phospholipid antigen.Key words: liposomes, antibodies, phospholipids, phosphatidylserine, phosphatidic acid.

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Bartlett, Marilyn S., William C. Angus, Margaret M. Shaw, et al. "Antibody to Pneumocystis cariniiProtects Rats and Mice from Developing Pneumonia." Clinical Diagnostic Laboratory Immunology 5, no. 1 (1998): 74–77. http://dx.doi.org/10.1128/cdli.5.1.74-77.1998.

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ABSTRACT Well-proven mouse and rat models were used to show that polyclonal antisera to Pneumocystis carinii protect against P. carinii pneumonia. Antibodies were obtained from animals that were allowed to recover from severe P. carinii pneumonia after immunosuppression had been stopped and which then were given a booster injection of P. carinii from the same animal species. Mice immunosuppressed with corticosteroids or antibodies to L3T4+ lymphocytes (which are comparable to CD4 cells of humans) and transtracheally inoculated with mouse P. carinii did not develop P. carinii pneumonia if they were passively immunized with antiserum, while mice immunosuppressed and inoculated by identical procedures but not given antibodies developed severe infections. Rats immunosuppressed with corticosteroids and inoculated with rat P. carinii had less severe infections if they were given rat anti-P. carinii antisera. The polyclonal antisera developed in mice provided greater protection for the mice than the polyclonal rat antisera did for the rats; however, the potencies and compositions of the antisera were not quantitated and probably differed. Since both rats and mice can be protected from P. carinii infections with polyclonal antisera, it may be possible to develop vaccines that will elicit protective antibodies in humans.

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Hawkins, K. L., R. V. Lloyd, and K. A. Toy. "Immunohistochemical Localization of Chromogranin A in Normal Tissues from Laboratory Animals." Veterinary Pathology 26, no. 6 (1989): 488–98. http://dx.doi.org/10.1177/030098588902600605.

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To analyze the distribution of Chromogranin A in endocrine cells of various species of laboratory animals (dog, gerbil, guinea pig, hamster, monkey, mouse, and fetal, neonatal, and adult rats), normal tissues were stained immunohistochemically with polyclonal anti-bovine Chromogranin A antiserum (SP-1). Selected tissues (pituitary, adrenal, thyroid, parathyroid, pancreas, brain, peripheral nerve, stomach, small and large intestine, bone marrow, spleen, thymus, lymph node, and liver) from these species and from the rabbit were stained with two monoclonal anti-human Chromogranin A antibodies (LK2H10 and PHE5) to compare the immunoreactivities of the monoclonal antibodies and polyclonal antiserum. Staining with the polyclonal antiserum (SP-1) resulted in a broader spectrum of immunoreactivity but had more nonspecific background staining than either monoclonal antibody. Immunoreactivity and staining intensity with SP-1 varied between species, but most endocrine tissues (pituitary cells in the anterior and intermediate lobes, thyroid “C” cells, adrenal medulla, parathyroid, pancreatic islets, and enterochromaffin cells) from most species stained positively. In some species, pancreatic alpha cells stained more intensely, and two populations of adrenal medullary cells with different staining intensities were observed. Sciatic nerve (axonal area) was immunoreactive with monoclonal antibodies and/or the polyclonal antiserum in several species. The spectrum of immunoreactive tissues from fetal and neonatal rats increased with age. There was good cross-reactivity between species with SP-1, but not with either LK2H10 or PHE5. These results indicate that many endocrine cells with secretory granules in laboratory animals express Chromogranin A and that a polyclonal antiserum, such as SP-1, is more sensitive in detecting this protein in various species than monoclonal antibodies such as LK2H10 or PHE5.

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Webster, D. E., D. L. Beck, F. Rabenstein, R. L. S. Forster, and P. L. Guy. "An improved polyclonal antiserum for detecting Ryegrass mosaic rymovirus." Archives of Virology 150, no. 9 (2005): 1921–26. http://dx.doi.org/10.1007/s00705-005-0531-z.

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Jürgens, G., A. Hermann, D. Aktuna, and W. Petek. "Dissociation-Enhanced Lanthanide Fluorescence Immunoassay of Lipoprotein(a) in Serum." Clinical Chemistry 38, no. 6 (1992): 853–59. http://dx.doi.org/10.1093/clinchem/38.6.853.

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Abstract Lipoprotein(a), a human serum lipoprotein structurally related to low-density lipoprotein (LDL), contains in addition to apolipoprotein B (apo B) apolipoprotein(a) [apo(a)], a glycoprotein with a strong homology to plasminogen. Lp(a) is a risk factor for coronary heart disease and ischemic cerebrovascular disease. Several immunological techniques are used to quantify Lp(a) in human serum, including radioimmunoassays, rocket immunoelectrophoresis, and enzyme-linked immunosorbent assays. Only the last method is suitable for large-scale clinical studies. We describe another solid-phase immunoassay, based on the dissociation-enhanced lanthanide fluorescence system Delfia (Wallac Oy), and outline the technical details. A polyclonal antiserum directed against Lp(a) was used as the capture antibody. Two kinds of detection antibodies were applied, a polyclonal antiserum against apo B and the polyclonal antiserum against Lp(a). The results agree excellently with the values estimated by rocket immunoelectrophoresis. This assay is easily established, measures Lp(a) in a wide concentration range, and is suitable for screening large populations.

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Kipnis, T. L., D. V. Tambourgi, M. J. M. Alves, and W. Dias da Silva. "Comparison of the C-mediating killing activity and C-activating properties of mouse monoclonal and polyclonal antibodies against Trypanosoma cruzi." Mediators of Inflammation 1, no. 5 (1992): 309–12. http://dx.doi.org/10.1155/s0962935192000450.

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A Mouse polyclonal antiserum against Trypanosoma cruzi or its IgG and IgM fractions and five monoclonal antibodies (two IgM, two IgG1and one IgG2a) recognize and combine with membrane components of trypomastigote forms of the parasite as revealed by immunofluorescence. Although all these antibodies sensitize trypomastigotes and prepare them to activate the complement (C) system, as measured by consumption of total C, C4, B and C3, only the polyclonal antiserum or its IgG, IgM and Fabμ fragments were able to induce trypanosome lysis by the alternative C pathway.

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Mohsin, Aliah Zannierah, Rashidah Sukor, Jinap Selamat та ін. "Generation of High Affinity Anti-Peptide Polyclonal Antibodies Recognizing Goat αs1-Casein". Molecules 25, № 11 (2020): 2622. http://dx.doi.org/10.3390/molecules25112622.

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The chemical, technological and allergy properties of goat’s milk are significantly affected by the level of αs1-casein. Detection and quantification of αs1-casein requires high-specificity methods to overcome high-sequence similarity between this protein and others in the casein family. Unavailability of antibodies with high affinity and specificity towards goat αs1-casein hinders the development of immuno-based analytical methods such as enzyme-linked immunosorbent assay (ELISA) and biosensors. Here, we report the generation of polyclonal antibodies (or immunoglobulins, IgGs) raised towards goat αs1-casein N- (Nter) and C-terminal (Cter) peptide sequences. The Nter and Cter peptides of goat αs1-casein were immunized in rabbits for the generation of antisera, which were purified using protein G affinity chromatography. The binding affinity of the antisera and purified IgGs were tested and compared using indirect ELISA, where peptide-BSA conjugates and goat αs1-casein were used as the coating antigens. The Nter antiserum displayed higher titer than Cter antiserum, at 1/64,000 and 1/32,000 dilutions, respectively. The purification step further yielded 0.5 mg/mL of purified IgGs from 3 mL of antisera. The purified Nter IgG showed a significantly (p < 0.05) higher binding affinity towards peptide-BSA and goat αs1-casein, with lower Kd value at 5.063 × 10−3 μM compared to 9.046 × 10−3 μM for the Cter IgG. A cross-reactivity test showed that there was no binding in neither Nter nor Cter IgGs towards protein extracts from the milk of cow, buffalo, horse and camel. High-quality antibodies generated will allow further development of immuno-based analytical methods and future in vitro studies to be conducted on goat αs1-casein.

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Oliveira, Tereza Cristina R. M. de, and Elisa Yoko Hirooka. "Low cost production and purification of polyclonal antibodies to staphylococcal enterotoxin A." Revista de Microbiologia 30, no. 2 (1999): 120–24. http://dx.doi.org/10.1590/s0001-37141999000200006.

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An immunization scheme for production of antiserum to staphylococcal enterotoxin A (SEA) is proposed. The reference method of Robbins and Bergdoll was modified to reduce the number of doses and the amount of toxin used per animal. The best immunization scheme used injections in days 0, 8, 24, 59, 62 and 67. The amount of toxin at each injection was 5, 6, 20, 50, 100 and 200mg, respectively. The total amount of toxin was 381mg, which corresponded to a reduction of 107mg in the amount of toxin for each animal when compared to the reference method. The average antiserum titer using the Optimum Sensitivity Plate - OSP was 1:60 and using ELISA the titer was 1:100.000. The lack of cross-reactivity with other staphylococcal enterotoxins indicated high specificity of the antibody to SEA. The proposed immunization scheme was adequate to produce specific SEA antisera, with high titers and the aditional advantage of reducing the amount of purified SEA required for immunization.

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Sherratt, T. G., T. Vulliamy, and P. N. Strong. "Evolutionary conservation of the dystrophin central rod domain." Biochemical Journal 287, no. 3 (1992): 755–59. http://dx.doi.org/10.1042/bj2870755.

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Dystrophin cDNA fragments encoding the C-terminal repeats of the central rod region have been expressed as fusion proteins. The polyclonal antisera raised to the purified fusion proteins have been characterized and neither antiserum cross-reacted with dystrophin-related protein. Antisera detected dystrophin with molecular mass close to that of the human in all terrestrial vertebrates and amphibia studied. Experiments with antisera to the N-terminal region of the dystrophin rod confirmed that epitopes to the rod region were conserved during this evolutionary period and the length of this domain remained unaltered.

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Lauweryns, J. M., L. van Ranst, R. V. Lloyd, and D. T. O'Connor. "Chromogranin in bronchopulmonary neuroendocrine cells. Immunocytochemical detection in human, monkey, and pig respiratory mucosa." Journal of Histochemistry & Cytochemistry 35, no. 1 (1987): 113–18. http://dx.doi.org/10.1177/35.1.3098831.

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Immunoreactive chromogranin A was demonstrated by immunocytochemistry in the cytoplasm of neuroendocrine cells (NEC) and neuroepithelial bodies (NEB) in human, monkey, and pig respiratory mucosa. Three different antisera (one monoclonal and one polyclonal to human chromogranin A, and one polyclonal to bovine chromogranin A) were applied in this study. Chromogranin immunopositivity varied in extent and intensity according to the antiserum applied and the tissue investigated. The monoclonal antibody revealed the strongest immunoreaction. Good correlation between chromogranin immunoreactivity and Grimelius silver staining was observed by comparing adjacent sections, although more cells seemed to reveal chromogranin immunoreactivity than argyrophylia. Chromogranin appears to be a useful histological marker for APUD cells in the respiratory mucosa of several species.

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Reynolds, G. M., D. C. Rowlands, and G. P. Mead. "Detection of Ki67 antigen by a new sheep polyclonal antiserum." Journal of Clinical Pathology 48, no. 12 (1995): 1138–40. http://dx.doi.org/10.1136/jcp.48.12.1138.

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Vos, J. H., T. S. G. A. M. van den Ingh, W. Misdorp, F. C. S. Ramaekers, F. N. van Mil, and M. Neijs. "Keratin Staining of Canine Epithelial Tissues by a Polyclonal Antiserum." Journal of Veterinary Medicine Series A 36, no. 1-10 (1989): 374–85. http://dx.doi.org/10.1111/j.1439-0442.1989.tb00743.x.

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Duan, Peng, Ye Xu, Barbara Birkaya, et al. "Generation of polyclonal antiserum for the detection of methylarginine proteins." Journal of Immunological Methods 320, no. 1-2 (2007): 132–42. http://dx.doi.org/10.1016/j.jim.2007.01.006.

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Lin, Jun, Joseph S. Hogan, and K. Larry Smith. "Antigenic Homology of the Inducible Ferric Citrate Receptor (FecA) of Coliform Bacteria Isolated from Herds with Naturally Occurring Bovine Intramammary Infections." Clinical Diagnostic Laboratory Immunology 6, no. 6 (1999): 966–69. http://dx.doi.org/10.1128/cdli.6.6.966-969.1999.

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ABSTRACT Expression of ferric citrate receptor FecA by Escherichia coli and Klebsiella pneumoniae isolated from bovine mastitis was investigated. Transformant E. coliUT5600/pSV66, which produces large quantities of FecA in the presence of citrate, was constructed. The FecA of E. coliUT5600/pSV66 was purified by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and used to prepare polyclonal antiserum in rabbits. All coliform isolates of E. coli (n = 18) and K. pneumoniae(n = 17) from naturally occurring bovine intramammary infections in five herds induced iron-regulated outer membrane proteins when grown in Trypticase soy broth containing 200 μM α-α′-dipyridyl and 1 mM citrate. Polyclonal antiserum against FecA was used in conjunction with an immunoblot technique to determine the degree of antigenic homology of FecA among isolates. In the presence of citrate, each isolate expressed FecA that reacted with the anti-FecA polyclonal antiserum. The molecular mass of FecA (∼80.5 kDa) was also highly conserved among isolates. Therefore, the ferric citrate iron transport may be induced in coliform bacteria and utilized to acquire iron in milk for survival and growth. The FecA is an attractive vaccine component for controlling coliform mastitis during the lactation period.

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Mumford, Andrew, Daxin Chen, Anthony Dorling, Geoffrey Kemball-Cook, and John McVey. "Generation of a polyclonal rabbit anti-mouse tissue factor antibody by nucleic acid immunisation." Thrombosis and Haemostasis 93, no. 01 (2005): 160–64. http://dx.doi.org/10.1160/th03-11-0703.

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SummaryTissue factor (TF) the cellular receptor and cofactor for factor VII, initiates coagulation and has also been implicated in several coagulation-independent functions, including inflammation, angiogenesis and tumour metastasis. Investigations of TF expression in mouse models of these processes has been limited by the availability of antibodies that specifically recognise mouse TF.We have generated a rabbit polyclonal antibody to mTF by DNA immunisation. This has yielded an antiserum that recognises native mTF in immunohistochemical and flow cytometric analyses.Furthermore,the antiserum is inhibitory in coagulation assays.This antiserum will be a valuable investigative tool in the analysis of mTF expression.

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Eriksson, B., H. Arnberg, K. Öberg, et al. "A polyclonal antiserum against chromogranin A and B - a new sensitive marker for neuroendocrine tumours." Acta Endocrinologica 122, no. 2 (1990): 145–55. http://dx.doi.org/10.1530/acta.0.1220145.

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Abstract Chromogranins A, B, and C, proteins that are co-stored and co-released with peptides and amines, have been identified in a variety of neuroendocrine tissues, both normal and neoplastic. We examined the secretion of chromogranin A and chromogranin A + B by hormone-producing tumours in patients with endocrine pancreatic tumours, carcinoid tumours, pheochromocytomas, and small cell lung cancer. The radioimmunoassay determining the plasma concentrations of chromogranin A + B showed a greater sensitivity than that determining chromogranin A alone. All patients with endocrine pancreatic tumours, carcinoids, and pheochromocytomas had increased levels of chromograin A + B, whereas a small number of the patients (5/18 with endocrine pancreatic tumours and ⅓ with pheochromocytomas) had normal levels of chromogranin A. Also in immunocytochemical stainings, our polyclonal antiserum detecting both chromogranin A and B showed a greater sensitivity than other available antisera against chromogranin A, B and C. We have demonstrated that a polyclonal antiserum against a mixture of chromogranin A and B might be a more sensitive marker than chromogranin A alone for diagnosing neuroendocrine tumours. This is not surprising, since both chromogranins are widely distributed in neuroendocrine cells.

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Basso, Marcos Fernando, Álvaro Júlio Pereira, Hermano Monteiro de Barros Pereira, et al. "Screening of papaya accessions resistant to Papaya lethal yellowing virus and capacity of Tetranychus urticae to transmit the virus." Pesquisa Agropecuária Brasileira 50, no. 2 (2015): 97–105. http://dx.doi.org/10.1590/s0100-204x2015000200001.

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The objective of this work was to produce a polyclonal antiserum against the coat protein (CP) of Papaya lethal yellowing virus (PLYV) and to determine its specificity and sensibility in the diagnosis of the virus, as well as to evaluate the genetic resistance to PLYV in papaya (Carica papaya) accessions and to investigate the capacity of the two-spotted spider mite Tetranychus urticae to acquire and transmit PLYV to the plants. Sixty-five papaya accessions were evaluated. For each accession, ten plants were mechanically inoculated using PLYV-infected plant extracts, and three plants were mock inoculated with phosphate buffer alone and used as negative controls. Ninety days after inoculation, newly-emerging systemic leaves were collected from the inoculated plants, and viral infection was diagnosed by indirect Elisa, using polyclonal antiserum sensible to the in vitro-expressed PLYV CP. Viral transmission by T. urticae was evaluated in greenhouse. The experiments were repeated twice. Polyclonal antiserum recognized the recombinant PLYV CP specifically and discriminated PLYV infection from infections caused by other plant viruses. Out of the 65 papaya accessions evaluated, 15 were considered resistant, 18 moderately resistant, and 32 susceptible. The two-spotted spider mite T. urticae was capable of acquiring PLYV, but not of transmitting it to papaya.

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Monis, Judit, and Richard K. Bestwick. "Serological Detection of Grapevine Associated Closteroviruses in Infected Grapevine Cultivars." Plant Disease 81, no. 7 (1997): 802–8. http://dx.doi.org/10.1094/pdis.1997.81.7.802.

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Western blot immunoassay and enzyme-linked immunosorbent assay using different monoclonal antibodies (MAb) and polyclonal antisera (PA) revealed mixed infections of serologically related and unrelated grapevine leafroll associated viruses (GLRaVs) and grapevine corky bark associated virus (GCBaV) in symptomatic grapevines. A PA designated rootstock-scion incompatibility (RSI)-24 kDa, grapevine corky bark PA, and GLRaV-2b MAb reacted to polypeptides of approximately 24 kDa isolated from grapevines exhibiting rootstock-scion incompatibility, leafroll, and corky bark disease symptoms, suggesting that these isolates are infected with closely related viruses. A PA designated GLRaV-2 US detected virus specific polypeptides of 38, 37, 36, and 24 kDa, while a polyclonal antiserum designated GLRaV-2 FR detected a single virus-specific polypeptide of approximately 24 kDa. The reactivity of GLRaV-2 US to various polypeptides suggests that the immunogen used to produce this antiserum was a mixture of viruses. Apical meristems were excised and cultured to eliminate the infection of viruses in the grapevines showing RSI symptoms and in the cultivar French Colombard infected with GLRaV-1. The elimination of these viruses was confirmed by Western blot assay. These studies show that the Western blot assay can be used to detect and differentiate grapevine disease-associated closteroviruses.

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Liu, Shilian, Huaiji Yang, and Dexian Zheng. "Mitogenic Effect of Polyclonal Anti-Porcine Lymphocyte E-Receptor Antiserum IgG." Immunological Investigations 16, no. 5 (1987): 363–70. http://dx.doi.org/10.3109/08820138709087091.

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ZHANG, Qiliang, Zhenyi WANG, and Yelu XU. "Measurement of rabbit von willebrand factor antigen using specific polyclonal antiserum." Blood & Vessel 19, no. 4 (1988): 358–67. http://dx.doi.org/10.2491/jjsth1970.19.358.

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Chambliss, Ken L., and K. Michael Gibson. "Succinic semialdehyde dehydrogenase from mammalian brain: Subunit analysis using polyclonal antiserum." International Journal of Biochemistry 24, no. 9 (1992): 1493–99. http://dx.doi.org/10.1016/0020-711x(92)90077-e.

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Sadaghiani, Bahram, Bruce J. Crawford, and Juergen R. Vielkind. "Generation of poly- and mono-clonal antibodies against trout fibronectin (FN) and their use in FN immunodetection in teleost fishes." Biochemistry and Cell Biology 72, no. 7-8 (1994): 343–48. http://dx.doi.org/10.1139/o94-047.

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Immunization of rats with gelatin-affinity column purified fibronectin (FN) from rainbow trout (Oncorhynchus mykiss) plasma produced a polyclonal antiserum that reacts specifically with FN in immunoblotted protein extracts and cultured cells, not only from trout but also from swordtails (Xiphophorus helleri). Most importantly, this antiserum specifically stains FN-containing structures in sections from embryos, as well as skin and dorsal fin of swordtails and platyfish (Xiphophorus maculatus), allowing, e.g., correlation of the distribution of FN with neural crest cell development in Xiphophorus. The antiserum also cross-reacts with FN in sections from embroys of the Japanese medaka (Oryzias latipes) and coho salmon (Oncorhynchus kisutch). In addition to the polyclonal antibodies, monoclonal anti-trout FN antibodies were produced in rats. These did not exhibit reactivity on sections, but stained the cultured fish cells and FN in immunoblots. Both types of antibodies may be of interest to the fish industry for marking the level of FN as an indicator, not only for infectious diseases but also for certain developmental stages such as smoltification and spawning.Key words: antibodies, extracellular matrix, neural crest, Xiphophorus.

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Wen-Tao, Xu, Huang Kun-Lun, Deng Ai-Ke, and Luo Yun-Bo. "Enzyme linked immunosorbent assay for PAT protein detection in genetically modified rape." Chinese Journal of Agricultural Biotechnology 3, no. 3 (2006): 177–81. http://dx.doi.org/10.1079/cjb2006106.

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AbstractWe have developed and applied an immunoassay method to detect genetically modified (GM) rape containing phosphinothricin acetyltransferase (PAT). The purified PAT was identified by Western blotting and enzymic activity analysis. The polyclonal antibody against purified PAT protein was obtained and purified by both a saturated ammonium sulphate method and protein A-Sepharose 4B. The sensitivity and cross-reactivity of the polyclonal antibody has been demonstrated in an enzyme-linked immunosorbent assay (ELISA). The result of the ELISA for antiserum sensitivity was about 2×10−5mg/ml and the cross-reactivity determined experimentally showed a high degree of specificity for the antiserum used, because values were all less than 0.1%. Detection of transgenic plants was evaluated using two transgenic rape lines (MS1/RF1 and MS8/RF3) which could be easily distinguished by ELISA.

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Han, Lei, Shaoyu He, Jie Dong, Ye Wang, Jiaxing Huang, and Jie Wu. "First Characterization of Sphingomyeline Phosphodiesterase Expression in the Bumblebee, Bombus lantschouensis." Sociobiology 64, no. 1 (2017): 85. http://dx.doi.org/10.13102/sociobiology.v64i1.1256.

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The bumblebee (Bombus lantschouensis Vogt) is an important pollinator of wild plants. Sphingomyelin phosphodiesterase (SMPD) is a hydrolase that plays a major role in sphingolipid metabolism reactions. We report the preparation and characterization of a polyclonal antibody for bumblebee SMPD. We then use the polyclonal antiserum to detect the SMPD protein at different development stages and in different tissues. Our results showed that a 1228bp fragment homologous with the B. terrestris SMPD gene was successfully amplified. The molecular weight of the fusion protein was about 70 kDa by SDS-PAGE. An effective polyclonal antibody against SMPD was also obtained from mice and found to have a higher specificity for bumblebee SMPD. Western blotting detection showed that SMPD was expressed at a high level in queen ovaries, although expression was lower in the midgut and venom gland. SMPD expression decreased from the egg stage until the pdd stage. We interpret our results as showing that the development of an effective polyclonal antiserum for the SMPD protein of a bumblebee, which provides a tool for exploring the function of the SMPD gene. In addition, the work has confirmed that SMPD should be considered as an important enzyme during bumblebee egg and larval stages.

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Hempelmann, E., B. Putfarken, K. Rangachari, and R. J. M. Wilson. "Immunoprecipitation of malarial acid endopeptidase." Parasitology 92, no. 2 (1986): 305–12. http://dx.doi.org/10.1017/s0031182000064076.

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SUMMARYElectrophoresis of extracts of schizonts of Plasmodium knowlesi in non-dissociating polyacrylamide gels, separates several bands of acid endopeptidase activity. A polyclonal antiserum, produced by immunization with purified merozoites, failed to distinguish between different bands of the parasite enzyme, indicating that they are serologically related. Apart from the loss of one minor peak, extraction in Triton X-100 did not reduce the enzyme's electrophoretic heterogeneity. The antiserum did not react with red cell acid proteases.

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Verjan, Noel, Ikuo Hirono, and Takashi Aoki. "Genetic Loci of Major Antigenic Protein Genes of Edwardsiella tarda." Applied and Environmental Microbiology 71, no. 9 (2005): 5654–58. http://dx.doi.org/10.1128/aem.71.9.5654-5658.2005.

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ABSTRACT Seven antigenic proteins of Edwardsiella tarda were identified by using a rabbit polyclonal antiserum. Four of these proteins also reacted with a Japanese flounder antiserum. The amino acid sequences had identity to lipoproteins, periplasmic proteins, and exported and secreted proteins with roles in transport of metabolites across the cell membrane, stress response, and motility. These genes and their products are useful for developing DNA or recombinant subunit vaccines to control edwardsiellosis.

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van Lookeren Campagne, M., A. B. Oestreicher, T. P. van der Krift, W. H. Gispen, and A. J. Verkleij. "Freeze-substitution and Lowicryl HM20 embedding of fixed rat brain: suitability for immunogold ultrastructural localization of neural antigens." Journal of Histochemistry & Cytochemistry 39, no. 9 (1991): 1267–79. http://dx.doi.org/10.1177/39.9.1833448.

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We examined the suitability of freeze-substitution and Lowicryl HM20 embedding of aldehyde-fixed rat brain to localize several neural antigens at the ultrastructural level. The following rabbit polyclonal and mouse monoclonal antibodies were used: affinity-purified polyclonal immunoglobulins G raised to B-50/GAP43 (a membrane-anchored, growth-associated protein); affinity-purified polyclonal immunoglobulins G to human glial fibrillary acidic protein (GFAP; a subunit of glial filaments); a polyclonal antiserum raised to adrenocorticotropic hormone[25-39] (a neuropeptide present in dense-core granules); a polyclonal antiserum raised to myelin basic protein (a protein present in compact myelin of the central nervous system); and mouse monoclonal antibodies to synaptophysin (an integral membrane protein of small synaptic vesicles). Rat mesencephalon was fixed by perfusion with buffered 2% glutaraldehyde and 4% paraformaldehyde, cryoprotected, and frozen in liquid nitrogen. Freeze-substitution of tissue was performed with anhydrous methanol and 0.5% uranyl acetate at -90 degrees C. Semi-thin Lowicryl sections were used for light microscopic visualization of B-50 in the ventromedial mesencephalic central gray substance. The procedure preserves well the ultrastructure of this region and the immunoreactivity of the selected antigens. This study shows that dehydration by freeze-substitution, combined with Lowicryl HM20 embedding at sub-zero temperature, provides a successful method of preparation of fixed brain tissue for ultrastructural studies, allowing immunogold localization of several neural antigens by double labeling in the same section and in serial sections.

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Russell, V. E., U. Klein, M. Reuveni, D. D. Spaeth, M. G. Wolfersberger, and W. R. Harvey. "Antibodies to mammalian and plant V-ATPases cross react with the V-ATPase of insect cation-transporting plasma membranes." Journal of Experimental Biology 166, no. 1 (1992): 131–43. http://dx.doi.org/10.1242/jeb.166.1.131.

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In immunobiochemical blots, polyclonal antibodies against subunits of plant and mammalian vacuolar-type ATPases (V-ATPases) cross-react strongly with corresponding subunits of larval Manduca sexta midgut plasma membrane V-ATPase. Thus, rabbit antiserum against Kalanchoe daigremontiana tonoplast V-ATPase holoenzyme cross-reacts with the 67, 56, 40, 28 and 20 kDa subunits of midgut V-ATPase separated by SDS-PAGE. Antisera against bovine chromaffin granule 72 and 39 kDa V-ATPase subunits cross-react with the corresponding 67 and 43 kDa subunits of midgut V-ATPase. Antisera against the 57 kDa subunit of both beet root and oat root V-ATPase cross-react strongly with the midgut 56 kDa V-ATPase subunit. In immunocytochemical light micrographs, antiserum against the beet root 57 kDa V-ATPase subunit labels the goblet cell apical membrane of both posterior and anterior midgut in freeze-substituted and fixed sections. The plant antiserum also labels the apical brush-border plasma membrane of Malpighian tubules. The ability of antibodies against plant V-ATPase to label these insect membranes suggests a high sequence homology between V-ATPases from plants and insects. Both of the antibody-labelled insect membranes transport K+ and both membranes possess F1-like particles, portasomes, on their cytoplasmic surfaces. This immunolabelling by xenic V-ATPase antisera of two insect cation-transporting membranes suggests that the portasomes on these membranes may be V-ATPase particles, similar to those reported on V-ATPase-containing vacuolar membranes from various sources.

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Griep, Remko A., Charlotte van Twisk, José R. C. M. van Beckhoven, Jan M. van der Wolf, and Arjen Schots. "Development of Specific Recombinant Monoclonal Antibodies Against the Lipopolysaccharide of Ralstonia solanacearum Race 3." Phytopathology® 88, no. 8 (1998): 795–803. http://dx.doi.org/10.1094/phyto.1998.88.8.795.

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Recombinant single-chain antibodies (scFvs) against the lipopolysaccharide of Ralstonia solanacearum (biovar 2, race 3) were successfully selected by phage display from a large combinatorial antibody library. Characterization with regard to cross-reaction and use in routine immunoassays showed that the selected antibodies had improved characteristics when compared with the polyclonal antiserum that is currently used for brown rot diagnosis of potato in the Netherlands. The isolated monoclonal scFvs reacted in both enzyme-linked immunosorbent assay (ELISA) and immunofluorescence cell staining with all race 3 strains tested, but with only some strains belonging to other races. Furthermore, only a few cross-reactions with saprophytic bacteria, which also cross-reacted with polyclonal antisera, were observed. Using ELISA, one of the recombinant antibodies detected as few as 5 × 103 bacteria in potato tuber extracts. Therefore, this antibody is potentially useful for detection of R. solanacearum race 3.

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Levine, SP, LK Knieriem, and MA Rager. "Platelet factor 4 and the platelet secreted proteoglycan: immunologic characterization by crossed immunoelectrophoresis." Blood 75, no. 4 (1990): 902–10. http://dx.doi.org/10.1182/blood.v75.4.902.902.

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Abstract Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent antiheparin activity. It also binds to a chondroitin sulfate- containing proteoglycan (PG) isolated from platelets. In order to evaluate further the relationship between PF4 and the chondroitin sulfate-containing proteoglycan in resting platelets, the PF4-binding proteoglycan from human platelets has been purified using purified PF4 as an affinity ligand and used to prepare polyclonal antiserum. Two antisera have been characterized: one reacts primarily with chondroitin sulfate (CS), the other reacts with the protein core of the platelet proteoglycan after chondroitinase AC digestion. PF4 and PG core protein antigen are present in separate, dissimilar precipitin arcs when triton- solubilized platelets are analyzed by crossed immunoelectrophoresis using polyclonal antisera to purified PF4 and PG. PF4 was demonstrated in a complex with a separate chondroitin sulfate antigen by crossed immunoelectrophoresis (CIE) experiments in which either anti-PF4 or anti-CS antisera was incorporated in the intermediate gel. Both the PF4- chondroitin sulfate complex and the proteoglycan are secreted from platelets when fresh, washed human platelets are stimulated by human alpha-thrombin. This second antigen may represent the PG after posttranslational modification of a precursor form of the proteoglycan.

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Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent antiheparin activity. It also binds to a chondroitin sulfate- containing proteoglycan (PG) isolated from platelets. In order to evaluate further the relationship between PF4 and the chondroitin sulfate-containing proteoglycan in resting platelets, the PF4-binding proteoglycan from human platelets has been purified using purified PF4 as an affinity ligand and used to prepare polyclonal antiserum. Two antisera have been characterized: one reacts primarily with chondroitin sulfate (CS), the other reacts with the protein core of the platelet proteoglycan after chondroitinase AC digestion. PF4 and PG core protein antigen are present in separate, dissimilar precipitin arcs when triton- solubilized platelets are analyzed by crossed immunoelectrophoresis using polyclonal antisera to purified PF4 and PG. PF4 was demonstrated in a complex with a separate chondroitin sulfate antigen by crossed immunoelectrophoresis (CIE) experiments in which either anti-PF4 or anti-CS antisera was incorporated in the intermediate gel. Both the PF4- chondroitin sulfate complex and the proteoglycan are secreted from platelets when fresh, washed human platelets are stimulated by human alpha-thrombin. This second antigen may represent the PG after posttranslational modification of a precursor form of the proteoglycan.

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Hajra, Tapas K., Prasanta K. Bag, Suresh C. Das, Souryadeep Mukherjee, Asis Khan, and T. Ramamurthy. "Development of a Simple Latex Agglutination Assay for Detection of Shiga Toxin-Producing Escherichia coli (STEC) by Using Polyclonal Antibody against STEC." Clinical and Vaccine Immunology 14, no. 5 (2007): 600–604. http://dx.doi.org/10.1128/cvi.00342-06.

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ABSTRACT Rabbit antiserum raised against the whole-cell antigen of Shiga toxin-producing Escherichia coli (STEC) strain VT3 (stx 1 + stx 2 + eae +) was repeatedly adsorbed with heat-killed cells of different non-STEC strains and other enteric bacteria. Thus, the antiserum obtained was designated VT3 antiserum. VT3 antiserum reacted with intimin type γ. We assessed the reactivity of VT3 antiserum to whole-cell lysates of 87 strains of E. coli and other enteric bacteria by immunoblotting. The antiserum recognized the 97-kDa protein in whole-cell lysate from strain VT3, and 36 (83.7%) of the 43 STEC strains were positive for the STEC antigen. None of the non-STEC strains or strains of other species examined tested positive by immunoblotting. Based on this result, we developed a latex agglutination assay for the detection of STEC strains. Thirty-five (81.4%) of the 43 STEC strains tested positive for the STEC antigen by the latex agglutination assay. One (3.3%) of the 30 non-STEC strains and none of the strains of the other enteric bacteria included in this study tested positive by the latex agglutination assay. The corresponding specificity of the latex agglutination assay was approximately 98%. Results of this study showed the production of STEC antiserum and the generation of a simple, cost-effective, sensitive, and specific latex agglutination assay for establishing an etiological diagnosis of STEC.

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Cavileer, T. D., R. C. Clarke, D. L. Corsini, and P. H. Berger. "A New Strain of Potato Carlavirus M." Plant Disease 82, no. 1 (1998): 98–102. http://dx.doi.org/10.1094/pdis.1998.82.1.98.

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In 1994, potato samples for certification from Idaho seed fields reacted in enzyme-linked immunosorbent assay (ELISA) tests to a polyclonal potato carlavirus M (PVM) antiserum. Sample affinity to the antiserum was lower than control samples. Furthermore, ELISA-positive samples were obtained from both symptomatic as well as asymptomatic plants. A complementary DNA library was prepared using both reverse transcription-polymerase chain reaction and primers based on published PVM sequences, or oligo d(T) primed reverse transcribed sequences. The nucleotide sequence was determined for the 3′-terminus of the genome. Putative coat protein amino acid sequence was compared to published PVM and potato virus S coat protein sequences. While this new isolate is likely a strain of PVM, it is significantly different from known PVM coat protein sequences in the amino terminus region. These differences may explain the poor reactivity to other PVM antisera and suggest that it is a new strain of PVM, which we have designated PVM-ID.

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Green, Brett James, Detlef Schmechel, and Euan Roger Tovey. "Detection of Aerosolized Alternaria alternata Conidia, Hyphae, and Fragments by Using a Novel Double-Immunostaining Technique." Clinical Diagnostic Laboratory Immunology 12, no. 9 (2005): 1114–16. http://dx.doi.org/10.1128/cdli.12.9.1114-1116.2005.

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ABSTRACT A double-immunostaining halogen immunoassay was developed to identify aerosolized conidia, hyphae, and fragments of Alternaria alternata by using an anti-Alternaria polyclonal antiserum, while, simultaneously, allergy to these components was concurrently determined by using human immunoglobulin E antibodies.

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Li, De-Kun, Ying-Tao Mu, and Huan-Huan Feng. "The expression and purification of LpxA of Chlamydia trachomatis and preparation of its polyclonal antibody." Zeitschrift für Naturforschung C 75, no. 9-10 (2020): 313–17. http://dx.doi.org/10.1515/znc-2020-0050.

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AbstractThe purpose of this study is to purify the LpxA protein of Chlamydia trachomatis (Ct) and prepare the polyclonal antibody against LpxA protein, so as to lay a foundation for studying the function of LpxA protein. The LpxA gene was amplified by PCR. The expression plasmid pET28a-LpxA was constructed by using pET28a as the vector. The fusion protein containing 6 histidine tag was induced by IPTG and purified by Ni2+ chromatography gel. The purified His-LpxA protein was used as an immunogen to immunize New Zealand rabbits subcutaneously through the back to prepare polyclonal antibody. Immunoblotting was used to detect the reaction between the antibody and His-LpxA. The determination of polyclonal antibody titer was detected by ELISA. The relative molecular weight of His-LpxA was 32.8 kDa, and it could be expressed in Escherichia coli. The purity of the purified protein was about 95%. After immunizing New Zealand rabbits, the antiserum was able to recognize the recombinant His-LpxA protein with a titer greater than 1:10240. In this study, LpxA protein was successfully purified and antiserum was prepared, which provided an experimental basis for studying the function of LpxA protein.

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Shuto, Yujin, Tamotsu Shibasaki, Ken Wada, et al. "Generation of polyclonal antiserum against the growth hormone secretagogue receptor (GHS-R)." Life Sciences 68, no. 9 (2001): 991–96. http://dx.doi.org/10.1016/s0024-3205(00)01001-8.

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Tenckhoff, Bernhard, H. W. Kölmel, V. Wolf, and R. Lange. "Production and characterization of a polyclonal antiserum against Spiroplasma mirum (ATCC 29335)." Zentralblatt für Bakteriologie 280, no. 3 (1994): 409–15. http://dx.doi.org/10.1016/s0934-8840(11)80605-5.

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Fanti, Paolo, Giovanna Colombo, Chinghua Yao, Stephen A. Brown, Michael W. Vernon, and Hartmut H. Malluche. "Development and characterization of a polyclonal antiserum-based radioimmunoassay for dog osteocalcin." Journal of Bone and Mineral Research 8, no. 6 (2009): 745–52. http://dx.doi.org/10.1002/jbmr.5650080613.

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Vaira, A. M., M. Vecchiati, V. Masenga, and G. P. Accotto. "A polyclonal antiserum against a recombinant viral protein combines specificity with versatility." Journal of Virological Methods 56, no. 2 (1996): 209–19. http://dx.doi.org/10.1016/0166-0934(95)01963-4.

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Chan-Palay, Victoria, and Gazi Yasargil. "Immunocytochemistry of human brain tissue with a polyclonal antiserum against neuropeptide Y." Anatomy and Embryology 174, no. 1 (1986): 27–33. http://dx.doi.org/10.1007/bf00318333.

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Gerner, M. L., G. V. Leontyeva, I. G. Romenskaya, M. S. Melnick, and M. L. Rabinovich. "A polyclonal antiserum to the noncatalytic part of cellobiohydrolase I fromTrichoderma reesei." Applied Biochemistry and Microbiology 36, no. 1 (2000): 1–3. http://dx.doi.org/10.1007/bf02738124.

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K. PECK, ROBERT, FRANÇOISE DUBORGEL, IRM HUTTENLAUCH, and GERARD DE HALLER. "The Membrane Skeleton of Pseudomicrothorax." Journal of Cell Science 100, no. 4 (1991): 693–706. http://dx.doi.org/10.1242/jcs.100.4.693.

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The epiplasm membrane skeleton of the ciliated protozoan Pseudomicrothorax dubius has been isolated and its three-dimensional structure and constituent proteins have been examined. The epiplasm functions as a cytoskeleton to define cell shape and the position of some cortical organelles. Scanning electron microscopy of the isolated epiplasm reveals a rococo cytoarchitecture in which basal bodies and trichocyst attachment sites are arranged in precise geometric arrays. SDS-PAGE reveals 40 bands, one of which is quantitatively the major band of the epiplasm and is composed of at least 3 different proteins and numerous isoelectric variants, as revealed by two-dimensional electrophoresis and peptide mapping. Polyclonal antisera were produced against native (antiserum 15) and SDS-denatured (antiserum 18) epiplasm. On immunoblots, antiserum 15 labels the hydrophilic proteins that are extracted from the epiplasm by treatment with dilute acid solution and that are predominantly glycoproteins, four of which are labeled with Concanavalin A on Western blots. On Lowicryl thin sections, antiserum 15 labels the epiplasm uniformly, except for the terminal plates, indicating that the glycoproteins are integral components of the epiplasm and are not membrane contaminants in the epiplasm fraction. Concanavalin A labeling of Lowicryl sections supports the latter result. On immunoblots, antiserum 18 labels the acid-insoluble epiplasm bands, the major structural elements of the epiplasm. One of the epiplasm bands at 52x1O3Mr is labeled by an anti-β tubulin monoclonal antibody. Evidence is presented that this β tubulin is not due to microtubule contamination of the epiplasm fraction.

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