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Journal articles on the topic 'Polypeptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Darr, S. C., S. C. Somerville, and C. J. Arntzen. "Monoclonal antibodies to the light-harvesting chlorophyll a/b protein complex of photosystem II." Journal of Cell Biology 103, no. 3 (1986): 733–40. http://dx.doi.org/10.1083/jcb.103.3.733.

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A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that t

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2

Machesky, L. M., S. J. Atkinson, C. Ampe, J. Vandekerckhove, and T. D. Pollard. "Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose." Journal of Cell Biology 127, no. 1 (1994): 107–15. http://dx.doi.org/10.1083/jcb.127.1.107.

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We identified four polypeptides of 47, 44, 40, and 35 kD that bind to profilin-Sepharose and elute with high salt. When purified by conventional chromatography using an antibody to the 47-kD polypeptide, these four polypeptides copurified as a stoichiometric complex together with three additional polypeptides of 19, 18, and 13 kD that varied in their proportions to the other polypeptides. Partial protein sequences showed that the 47-kD polypeptide is a homologue of S. pombe act2 and the 44-kD polypeptide is a homologue of S. cerevisiae ACT2, both unconventional actins. The 40-kD polypeptide co

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3

Geysen, J., J. Cardoen, and A. De Loof. "Distribution of yolk polypeptides in the follicle cells during the differentiation of the follicular epithelium in Sarcophaga bullata egg follicles." Development 101, no. 1 (1987): 33–43. http://dx.doi.org/10.1242/dev.101.1.33.

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In S. bullata, the ovaries contribute to the synthesis of yolk polypeptides. A specific antiserum for yolk polypeptides was used to visualize the presence of yolk polypeptides in the follicle cells during their differentiation. After vitellogenesis has started, all follicle cells contain yolk polypeptides. The squamous follicle cells covering the nurse cells and the border cells lose yolk polypeptides before mid-vitellogenesis, whereas the follicle cells over the oocyte contain yolk polypeptides until after late vitellogenesis. All follicle cells are immunonegative afterwards. In vitro transla

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4

Bodnar, Andrea G., and Richard A. Rachubinski. "Characterization of the integral membrane polypeptides of rat liver peroxisomes isolated from untreated and clofibrate-treated rats." Biochemistry and Cell Biology 69, no. 8 (1991): 499–508. http://dx.doi.org/10.1139/o91-074.

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We have characterized the integral membrane polypeptides of liver peroxisomes from untreated rats and rats treated with clofibrate, a peroxisome proliferator. Membranes, prepared by treatment of purified peroxisomes with sodium carbonate, were used to raise an antiserum in rabbits. Immunoblot analysis demonstrated the reaction of this antiserum with six peroxisomal integral membrane polypeptides (molecular masses, 140, 69, 50, 36, 22, and 15 kDa). Treatment of rats with the hypolipidemic drug clofibrate caused a 4- to 10-fold induction in the 69-kDa integral membrane polypeptide, while the oth

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5

Newsted, W. J., and N. P. A. Huner. "Major polypeptides associated with differentiation in psychrophilic fungi." Canadian Journal of Botany 65, no. 2 (1987): 233–41. http://dx.doi.org/10.1139/b87-033.

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Major polypeptides were observed upon one-dimensional sodium dodecyl sulfate gel electrophoresis of sclerotial extracts of the following psychrophiles: Myriosclerotinia borealis, Coprinus psychromorbidus, Typhula idahoensis, and Typhula incarnata. In general, the number, molecular mass, and relative proportion of these major sclerotial polypeptides varied considerably from species to species. Furthermore, in the case of M. borealis, the major sclerotial polypeptide did not appear to be an artifact of culturing conditions since a major polypeptide of similar molecular mass was also present in s

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6

Wheeler, R. A., Rex L. Smith, and D. A. Knauft. "Microsomal Polypeptide Comparisons Between High and Normal Oleic Acid Isogenic Peanut Lines Using Two-Dimensional Gel Electrophoresis1." Peanut Science 21, no. 1 (1994): 75–78. http://dx.doi.org/10.3146/i0095-3679-21-1-17.

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Abstract Peanut (Arachis hypogaea L. subsp. fastigiata var. vulgaris) developing seed microsomal polypeptides of the high oleic acid variant (F435) and its presumed isogenic, normal line (78-1339) were compared using two-dimensional gel electrophoresis. A pair of 20 kDa polypeptides focusing at pH 6.8 and 7.3 was present in all of the polypeptide profiles from both isolines regardless of maturity or genotype except for (F435) at stage 1 maturity. The stage 1 (F435) profile contained, instead, an 18 kDa polypeptide pair focusing at about pH 9.3. Based on correlation evidence, we postulate that

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7

Kim, W. K., N. K. Howes, and J. W. Martens. "Evidence for relatedness between Puccinia graminis f.sp. secalis and P. graminis f.sp. tritici from two-dimensional polypeptide mapping." Canadian Journal of Botany 65, no. 6 (1987): 1078–82. http://dx.doi.org/10.1139/b87-149.

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Two-dimensional electrophoretograms of detergent-soluble polypeptides extracted from dormant urediospores were used to compare interspecific and intraspecific relationships among nine races of rye stem rust (Puccinia graminis f.sp. secalis) and a hybrid between rye stem rust and wheat stem rust (P. graminis f.sp. tritici) and its parents. More than 280 polypeptides were detected in each race of rye stem rust. The nine races differed by one to five genes for virulence and by five to seven polypeptides, but these differences were not correlated. The rye–wheat stem rust hybrid, rye stem rust pare

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8

Kawchuk, L. M., W. K. Kim, and J. Nielsen. "A comparison of polypeptides from the wheat bunt fungi Tilletia laevis, T. tritici, and T. controversa." Canadian Journal of Botany 66, no. 12 (1988): 2367–76. http://dx.doi.org/10.1139/b88-321.

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Phenol-soluble polypeptides were extracted from teliospores of six races of each of Tilletia laevis and T. tritici, and eight collections of T. controversa. The polypeptides were separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis and the resulting patterns compared. Although the races and collections had the morphological and physiological features of their respective species and possessed different combinations of virulence genes, they all gave similar polypeptide patterns. There were 359 polypeptides common to all 20 races and collections. Another 56 polyp

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9

Dentler, W. L. "Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase." Journal of Cell Biology 107, no. 6 (1988): 2679–88. http://dx.doi.org/10.1083/jcb.107.6.2679.

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Cilia were isolated from Tetrahymena thermophila, extracted with Triton X-114, and the detergent-soluble membrane + matrix proteins separated into Triton X-114 aqueous and detergent phases. The aqueous phase polypeptides include a high molecular mass polypeptide previously identified as a membrane dynein, detergent-soluble alpha and beta tubulins, and numerous polypeptides distinct from those found in axonemes. Integral membrane proteins partition into the detergent phase and include two major polypeptides of 58 and 50 kD, a 49-kD polypeptide, and 5 polypeptides in relatively minor amounts. Th

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10

Enrich, C., O. Bachs, and W. H. Evans. "A 115 kDa calmodulin-binding protein is located in rat liver endosome fractions." Biochemical Journal 255, no. 3 (1988): 999–1005. http://dx.doi.org/10.1042/bj2550999.

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The distribution of calmodulin-binding polypeptides in various rat liver subcellular fractions was investigated. Plasma-membrane, endosome, Golgi and lysosome fractions were prepared by established procedures. The calmodulin-binding polypeptides present in the subcellular fractions were identified by using an overlay technique after transfer from gels to nitrocellulose sheets. Distinctive populations of calmodulin-binding polypeptides were present in all the fractions examined except lysosomes. A major 115 kDa calmodulin-binding polypeptide of pI 4.3 was located to the endosome subfractions, a

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11

Zhang, Chunlin, K. V. Nagaraja, V. Sivanandan, and J. A. Newman. "Identification and characterization of viral polypeptides from type-II avian adenoviruses." American Journal of Veterinary Research 52, no. 7 (1991): 1137–41. http://dx.doi.org/10.2460/ajvr.1991.52.07.1137.

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Summary The polypeptides of serologically related viruses of hemorrhagic enteritis (he) in turkeys, marble spleen disease (msd) in pheasants, and splenomegaly in chickens (smc) were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (sds-page) and analyzed by protein immunoblotting with polyclonal antibodies to he virus (hev). The viral polypeptides II, III, IV, V, VI, and VII were detected on sds-page with the size range from 18 to 97 kDa in hev. Viral polypeptides II, III, V, VI, and VII were detected in msd virus and virus of smc. Protein immunoblotting of viral proteins

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12

Peery, T., T. Shabat-Brand, R. Steinlauf, Y. Koltin, and J. Bruenn. "Virus-encoded toxin of Ustilago maydis: two polypeptides are essential for activity." Molecular and Cellular Biology 7, no. 1 (1987): 470–77. http://dx.doi.org/10.1128/mcb.7.1.470-477.1987.

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Cells of Ustilago maydis containing double-stranded RNA viruses secrete a virus-encoded toxin to which other cells of the same species and related species are sensitive. Mutants affected in the expression of the KP6 toxin were characterized, and all were viral mutants. A temperature-sensitive nonkiller mutant indicated that the toxin consists of two polypeptides, 12.5K and 10K, that are essential for the toxic activity. The temperature-sensitive nonkiller mutant was affected in the expression of the 10K polypeptide, and its toxic activity was restored by the addition of the 10K polypeptide to

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13

Peery, T., T. Shabat-Brand, R. Steinlauf, Y. Koltin, and J. Bruenn. "Virus-encoded toxin of Ustilago maydis: two polypeptides are essential for activity." Molecular and Cellular Biology 7, no. 1 (1987): 470–77. http://dx.doi.org/10.1128/mcb.7.1.470.

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Cells of Ustilago maydis containing double-stranded RNA viruses secrete a virus-encoded toxin to which other cells of the same species and related species are sensitive. Mutants affected in the expression of the KP6 toxin were characterized, and all were viral mutants. A temperature-sensitive nonkiller mutant indicated that the toxin consists of two polypeptides, 12.5K and 10K, that are essential for the toxic activity. The temperature-sensitive nonkiller mutant was affected in the expression of the 10K polypeptide, and its toxic activity was restored by the addition of the 10K polypeptide to

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14

Hirakata, M., J. Craft, and J. A. Hardin. "Autoantigenic epitopes of the B and D polypeptides of the U1 snRNP. Analysis of domains recognized by the Y12 monoclonal anti-Sm antibody and by patient sera." Journal of Immunology 150, no. 8 (1993): 3592–601. http://dx.doi.org/10.4049/jimmunol.150.8.3592.

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Abstract Anti-Sm antibodies, a specific marker for SLE, are directed against the B'/B and D polypeptides of Sm small nuclear ribonucleoproteins. The Y12 monoclonal anti-Sm antibody (Y12 mAb), as well as many anti-Sm patient sera, recognize cross-reactive epitopes on the B'/B and D polypeptides. This immunoreactive site is of special interest since polypeptides B and D share little amino acid sequence homology. In the present study, we have sought to establish the autoantigenic domain of polypeptides B and D that accounts for this epitope. We tested the ability of the Y12 mAb and anti-Sm sera t

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15

Heyting, C., A. J. J. Dietrich, P. B. Moens, et al. "Synaptonemal complex proteins." Genome 31, no. 1 (1989): 81–87. http://dx.doi.org/10.1139/g89-016.

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Synaptonemal complexes were isolated from rate spermatocytes for the purpose of biochemical and morphological analysis. Several monoclonal antibodies were elicited against purified synaptonemal complexes to study the composition and assembly of these structures. Four classes of antibodies could be discriminated according to the polypeptides that they recognize on Western blots of purified synaptonemal complexes, namely antibodies recognizing (i) a 190-kDa polypeptide; (ii) a 30- and a 33-kDa polypeptide; (iii) two polypeptides with molecular weights of about 120 kDa; and (iv) polypeptides with

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16

VEIJOLA, Johanna, Pia ANNUNEN, Peppi KOIVUNEN, Antony P. PAGE, Taina PIHLAJANIEMI та Kari I. KIVIRIKKO. "Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their β subunit". Biochemical Journal 317, № 3 (1996): 721–29. http://dx.doi.org/10.1042/bj3170721.

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Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the β subunit of prolyl 4-hydroxylases. We report here on the cloning and expression of the Caenorhabditis elegans PDI/β polypeptide and its isoform. The overall amino acid sequence identity and similarity between the processed human and C. elegans PDI/β polypeptides are 61% and 85% respectively, and those between the C. elegans PDI/β polypeptide and the PDI isoform 46% and 73%. The isoform differs from the PDI/β and ERp60 polypeptides in that its N-terminal thioredoxin-like domain has an unusu

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17

Giroux, Randal W., and W. Gary Filion. "A comparison of the chilling-stress response in two differentially tolerant cultivars of tomato (Lycopersicon esculentum)." Biochemistry and Cell Biology 70, no. 3-4 (1992): 191–98. http://dx.doi.org/10.1139/o92-029.

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The chilling responses of two differentially cold tolerant cultivars of tomato were monitored through in vivo labelling of polypeptides with [35S]methionine, both during a gradual temperature decrease (2 °C/day) and also during a rapid cold shock (4 °C). The polypeptides were separated by one-dimensional sodium dodecyl sulfate – polyacrylamide gel electrophoresis and revealed by fluorography. Both cultivars showed changes in the polypeptide profiles resulting from either chilling treatment. During the gradual temperature decrease, there were few differences exhibited between the two cultivars.

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18

Good, A. H., J. D. Craik, S. M. Jarvis, et al. "Characterization of monoclonal antibodies that recognize band 4.5 polypeptides associated with nucleoside transport in pig erythrocytes." Biochemical Journal 244, no. 3 (1987): 749–55. http://dx.doi.org/10.1042/bj2440749.

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Three monoclonal antibodies have been raised against partially purified band 4.5 polypeptides [Steck (1974) J. Cell Biol. 62, 1-19] from pig erythrocyte membranes. The antibodies were capable of binding to both intact pig erythrocytes and protein-depleted membrane preparations and recognized detergent-solubilized polypeptides from adult and neonatal pig erythrocytes that were photolabelled with [G-3H]nitrobenzylthioinosine (NBMPR), a potent specific inhibitor of nucleoside transport. The antibodies did not recognize polypeptides from neonatal pig erythrocytes that were photolabelled with the g

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19

Bolin, Steven R., and Julia F. Ridpath. "Range of viral neutralizing activity and molecular specificity of antibodies induced in cattle by inactivated bovine viral diarrhea virus vaccines." American Journal of Veterinary Research 51, no. 5 (1990): 703–7. http://dx.doi.org/10.2460/ajvr.1990.51.05.703.

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Summary The range of neutralizing activity to bovine viral diarrhea (bvd) virus and viral protein specificity of antibodies induced by 3 inactivated vaccines were evaluated by use of samples of sera obtained from 13 cattle 14 days after vaccination. Viral neutralizing antibodies were detected in all cattle to each of 10 noncytopathic and 10 cytopathic isolates of bvd virus. A viral-induced polypeptide (53,000 to 56,000 daltons) was detected by radioimmunoprecipitation with serum from all vaccinates. Other viral-induced polypeptides of 115,000, 80,000, 48,000, and 25,000 daltons were precipitat

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20

Frazer, I. H., I. R. Mackay, T. W. Jordan, S. Whittingham, and S. Marzuki. "Reactivity of anti-mitochondrial autoantibodies in primary biliary cirrhosis: definition of two novel mitochondrial polypeptide autoantigens." Journal of Immunology 135, no. 3 (1985): 1739–45. http://dx.doi.org/10.4049/jimmunol.135.3.1739.

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Abstract Sera that contained autoantibodies to mitochondria (AMA) by immunofluorescence were examined by immunoblotting for reactivity with mitochondrial polypeptides from various mammalian species, yeast, and E. coli. Mitochondrial polypeptides were separated by polyacrylamide gel electrophoresis, were immobilized on nitrocellulose, and were exposed to sera. The sera tested included 18 AMA-positive sera from patients with primary biliary cirrhosis (PBC), two AMA-positive sera from patients without PBC, and 53 AMA-negative sera. All AMA-positive sera reacted with either one or the other, or us

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21

Beresini, M. H., M. J. Lempert, and L. B. Epstein. "Overlapping polypeptide induction in human fibroblasts in response to treatment with interferon-alpha, interferon-gamma, interleukin 1 alpha, interleukin 1 beta, and tumor necrosis factor." Journal of Immunology 140, no. 2 (1988): 485–93. http://dx.doi.org/10.4049/jimmunol.140.2.485.

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Abstract Cytokine-induced polypeptides were identified in whole cell lysates of human fibroblasts by computer-based analysis of two-dimensional gels with the use of the PDQuest System. Treatment with interferon-alpha (IFN-alpha) and interferon-gamma (IFN-gamma) enhanced the synthesis of 12 and 28 polypeptides, respectively. Exposure to interleukin 1 alpha (IL-1 alpha) or interleukin 1 beta (IL-1 beta) resulted in the increased synthesis of seven identical polypeptides. Treatment with tumor necrosis factor (TNF) at 100 U/ml led to enhanced expression of seven polypeptides, whereas exposure to T

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22

Lin, H. B., S. M. Harley, J. M. Butler, and L. Beevers. "Multiplicity of clathrin light-chain-like polypeptides from developing pea (Pisum sativum L.) cotyledons." Journal of Cell Science 103, no. 4 (1992): 1127–37. http://dx.doi.org/10.1242/jcs.103.4.1127.

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A comparative study has been made of clathrin-coated vesicles from developing pea (Pisum sativum L.) cotyledons and bovine brains in order to characterize the clathrin light chains from a plant system. Four polypeptides of 31 kDa, 40 kDa, 46 kDa and 50 kDa are considered as candidates for clathrin light chains in the developing pea cotyledons. The 31 kDa, 40 kDa, 46 kDa and 50 kDa polypeptides, together with the 190 kDa heavy chain, are dissociated as triskelions when coated vesicles of developing pea cotyledons are treated with 2 M urea. Partially purified 46 kDa and 50 kDa polypeptides have

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23

Dedhar, S., and V. Gray. "Isolation of a novel integrin receptor mediating Arg-Gly-Asp-directed cell adhesion to fibronectin and type I collagen from human neuroblastoma cells. Association of a novel beta 1-related subunit with alpha v." Journal of Cell Biology 110, no. 6 (1990): 2185–93. http://dx.doi.org/10.1083/jcb.110.6.2185.

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We report the isolation from two human neuroblastoma cell lines of an Arg-Gly-Asp-dependent integrin complex capable of binding to vitronectin, fibronectin, and type I collagen. The two neuroblastoma cell lines, SK-N-SH and IMR-32, exhibit specific attachment to fibronectin and type I collagen. SK-N-SH cells exhibit a much stronger attachment to vitronectin than the IMR-32 cells, which attach poorly to this substrate. Affinity chromatography of octylglucoside extracts of 125I surface-labeled cells on GRGDSPK-Sepharose columns resulted in the specific binding and elution with GRGDSP of three ra

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24

Kirkness, E. F., та A. J. Turner. "Antibodies directed against a nonapeptide sequence of the γ-aminobutyrate (GABA)/benzodiazepine receptor α-subunit. Detection of a distinct α-like subunit in pig cerebral cortex but not cerebellum". Biochemical Journal 256, № 1 (1988): 291–94. http://dx.doi.org/10.1042/bj2560291.

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A synthetic peptide, corresponding to amino acid residues 101-109 of the bovine gamma-aminobutyrate/benzodiazepine receptor alpha-subunit, was used to raise a polyclonal antiserum. The reactivity of this antiserum towards polypeptides of both bovine and pig receptor preparations was established by immunoprecipitation and immunoblotting. Anti-peptide antibodies recognized the alpha-subunit (51 kDa) of receptor prepared from pig cerebellum or cerebral cortex. However, a polypeptide of 57 kDa was additionally recognized in cortical, but not cerebellar, preparations. This alpha-like polypeptide ap

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25

Kim, W. K., Michèle C. Heath, and R. Rohringer. "Comparative analysis of proteins of Uromyces phaseoli var. typica, U. phaseoli var. vignae, and U. viciae-fabae: polypeptide mapping by two-dimensional electrophoresis." Canadian Journal of Botany 63, no. 12 (1985): 2144–49. http://dx.doi.org/10.1139/b85-303.

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Proteins were extracted from urediospores of the bean rust fungus (Uromyces phaseoli var. typica: two isolates), of the cowpea rust fungus (U. phaseoli var. vignae; two isolates), and of the faba bean rust fungus (U. viciae-fabae; one isolate) and separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis under denaturing conditions. The two isolates of the cowpea rust fungus had identical polypeptide patterns; the two isolates of the bean rust fungus differed by 19 polypeptides. The polypeptide patterns of the bean rust, cowpea rust, and faba bean rust fungi differ

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26

Droppa, Magdolna, Jiri Masojidek, and Gábor Horváth. "Changes of the Polypeptide Composition in Thylakoid Membranes during Differentiation." Zeitschrift für Naturforschung C 45, no. 3-4 (1990): 253–57. http://dx.doi.org/10.1515/znc-1990-3-419.

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Changes in membrane polypeptide composition during greening of etiolated maize were investigated to confirm the existence of the developmental polypeptides of 12 - 15 kDa described recently in virescent soybean mutant [M. Droppa, M. L. Ghirardi, G. Horváth, and A. Melis, Biochim. Biophys. Acta 932, 138 - 145 (1988)]. These low molecular weight polypeptides were the most abundant proteins at the early stage of greening, but were largely absent from fully developed thylakoids. During greening the relative concentration of the 12-15 kDa polypeptides were inversely proportional to that of LHC II,

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27

Nawar, Hesham F., Natalie D. King-Lyons, John C. Hu, Raymond C. Pasek, and Terry D. Connell. "LT-IIc, a New Member of the Type II Heat-Labile Enterotoxin Family Encoded by an Escherichia coli Strain Obtained from a Nonmammalian Host." Infection and Immunity 78, no. 11 (2010): 4705–13. http://dx.doi.org/10.1128/iai.00730-10.

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ABSTRACT Two families of bacterial heat-labile enterotoxins (HLTs) have been described: the type I HLTs are comprised of cholera toxin (CT) of Vibrio cholerae, LT-I of Escherichia coli, and several related HLTs; the type II HLTs are comprised of LT-IIa and LT-IIb. Herein, we report LT-IIc, a new type II HLT encoded from an enterotoxigenic E. coli (ETEC) strain isolated from an avian host. Using a mouse Y1 adrenal cell bioassay, LT-IIc was shown to be less cytotoxic than CT, LT-IIa, or LT-IIb. Cytotoxicity of LT-IIc was partially neutralized by antisera recognizing LT-IIa or LT-IIb but not by a

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28

Sugane, Kazuo, Shu-Han Sun, and Tadashi Matsuura. "Radiolabelling of the excretory-secretory and somatic antigens of Anisakis simplex larvae." Journal of Helminthology 66, no. 4 (1992): 305–9. http://dx.doi.org/10.1017/s0022149x00014760.

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ABSTRACTAnisakis simplex larvae were cultured in vitro in medium containing 35-methionine for ten days. The medium and the larval tissues were analysed for biosynthetically labelled polypeptide by sodium dodecyl sulphate polyacrylamide gel electrophoresis and autoradiography. Immunoprecipitates with positive and negative human antisera were similarly analysed, using Staphylococcus aureus to absorb immunocomplexes. ES products of Anisakis larvae contained many polypeptides with molecular weights of less than 200 K. 180 KDa and 40 KDa polypeptides in ES products reacted with IgG in Anisakis-infe

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29

Yates, I. E., E. A. Carter, T. A. Wilkins, and B. W. Wood. "Seasonal Variation in Polypeptide Profiles and Cellular Structure of Pecan Leaves." Journal of the American Society for Horticultural Science 115, no. 6 (1990): 924–29. http://dx.doi.org/10.21273/jashs.115.6.924.

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Polypeptides from pecan [Carya illinoensis (Wangenh.) C. .Koch] leaves were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and visualized by silver staining. Pecan leaf protein profiles were similar irrespective of cultivar (Desirable and Stuart), leaflet position, reproductive status of the allied shoot, or seasonal leaf age relative to fruit development. The large subunit of ribulose l,5-bisphosphate carboxylase and the majority of the other polypeptides were consistently present. However, the most striking change in the polypeptide composition was the seasonal declin

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30

Jeng, Robert S., and Clive M. Brasier. "Two-dimensional mapping of mycelial polypeptides of Ophiostoma ulmi and Ophiostoma novo-ulmi, causal agents of Dutch elm disease." Canadian Journal of Botany 72, no. 3 (1994): 370–77. http://dx.doi.org/10.1139/b94-050.

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Two-dimensional mycelial polypeptide maps were used to compare interspecific and intraspecific relationships among six isolates of Ophiostoma ulmi and four Eurasian and four North American race isolates of Ophiostoma novo-ulmi. The basic polypeptide pattern of O. ulmi differs markedly from that of O. novo-ulmi. A number of polypeptides were identified that could differentiate the two species and one was detected that may discriminate Eurasian from North American races. Overall, a high degree of correlation between species, race, and polypeptides was evident. However, two O. ulmi isolates (MAB

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Mäkelä, T. P., K. Saksela, and K. Alitalo. "Two N-myc polypeptides with distinct amino termini encoded by the second and third exons of the gene." Molecular and Cellular Biology 9, no. 4 (1989): 1545–52. http://dx.doi.org/10.1128/mcb.9.4.1545-1552.1989.

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The N-myc and c-myc genes encode closely related nuclear phosphoproteins. We found that the N-myc protein from human tumor cell lines appears as four closely migrating polypeptide bands (p58 to p64) in sodium dodecyl sulfate-polyacrylamide gels. This and the recent finding that the c-myc protein is synthesized from two translational initiation sites located in the first and second exons of the gene (S. R. Hann, M. W. King, D. L. Bentley, C. W. Anderson, and R. N. Eisenman, Cell 52:185-195, 1988) prompted us to study the molecular basis of the N-myc protein heterogeneity. Dephosphorylation by a

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Mäkelä, T. P., K. Saksela, and K. Alitalo. "Two N-myc polypeptides with distinct amino termini encoded by the second and third exons of the gene." Molecular and Cellular Biology 9, no. 4 (1989): 1545–52. http://dx.doi.org/10.1128/mcb.9.4.1545.

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The N-myc and c-myc genes encode closely related nuclear phosphoproteins. We found that the N-myc protein from human tumor cell lines appears as four closely migrating polypeptide bands (p58 to p64) in sodium dodecyl sulfate-polyacrylamide gels. This and the recent finding that the c-myc protein is synthesized from two translational initiation sites located in the first and second exons of the gene (S. R. Hann, M. W. King, D. L. Bentley, C. W. Anderson, and R. N. Eisenman, Cell 52:185-195, 1988) prompted us to study the molecular basis of the N-myc protein heterogeneity. Dephosphorylation by a

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Suyama, K., and J. Goldstein. "Enzymatic evidence for differences in the placement of Rh antigens within the red cell membrane." Blood 75, no. 1 (1990): 255–60. http://dx.doi.org/10.1182/blood.v75.1.255.255.

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Abstract Intact erythrocytes of different Rh genotypes were subjected to various enzyme treatments, the effects of which were monitored by separating the membrane proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and performing Western blotting using an antibody preparation that recognizes only Rh-related polypeptides. We found that treatment of intact cells with either phospholipase A2 or proteases such as papain did not alter the size of Rh antigen-containing polypeptides. In contrast, phospholipase A2 treatment followed by papain digestion cleaved a fraction of these pol

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Suyama, K., and J. Goldstein. "Enzymatic evidence for differences in the placement of Rh antigens within the red cell membrane." Blood 75, no. 1 (1990): 255–60. http://dx.doi.org/10.1182/blood.v75.1.255.bloodjournal751255.

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Intact erythrocytes of different Rh genotypes were subjected to various enzyme treatments, the effects of which were monitored by separating the membrane proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and performing Western blotting using an antibody preparation that recognizes only Rh-related polypeptides. We found that treatment of intact cells with either phospholipase A2 or proteases such as papain did not alter the size of Rh antigen-containing polypeptides. In contrast, phospholipase A2 treatment followed by papain digestion cleaved a fraction of these polypeptides

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Lingappa, J. R., R. L. Martin, M. L. Wong, D. Ganem, W. J. Welch, and V. R. Lingappa. "A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle." Journal of Cell Biology 125, no. 1 (1994): 99–111. http://dx.doi.org/10.1083/jcb.125.1.99.

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We have established a system for assembly of hepatitis B virus capsid, a homomultimer of the viral core polypeptide, using cell-free transcription-linked translation. The mature particles that are produced are indistinguishable from authentic viral capsids by four criteria: velocity sedimentation, buoyant density, protease resistance, and electron microscopic appearance. Production of unassembled core polypeptides can be uncoupled from production of capsid particles by decreasing core mRNA concentration. Addition of excess unlabeled core polypeptides allows the chase of the unassembled polypep

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Rahman, S., B. Kosar-Hashemi, MS Samuel, et al. "The Major Proteins of Wheat Endosperm Starch Granules." Functional Plant Biology 22, no. 5 (1995): 793. http://dx.doi.org/10.1071/pp9950793.

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Wheat starch contains two classes of associated proteins: proteins which are embedded within the granule and loosely associated surface proteins. The characterisation of the major proteins that are embedded in the granule are described. Gel electrophoresis on the basis of size resolved these proteins into five bands of molecular weights 60, 75, 85, 100 and 105 kDa. These polypeptides were demonstrated to be within the granule by their resistance to proteinase K digestion when granules were ungelatinised. The N-terminal sequences of these polypeptides are reported. The most prominent polypeptid

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Okada, M., Y. Okabe, M. Kono, K. Nakayama, and H. Satoh. "Peptide composition and enzyme activities of isolated pyrenoids from the green alga Bryopsis maxima." Canadian Journal of Botany 69, no. 5 (1991): 1053–61. http://dx.doi.org/10.1139/b91-135.

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Pyrenoids of Bryopsis maxima contained several minor components other than the large subunit (LS) and the small subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). Among the minor components, polypeptides of 95, 67, and 41 kDa reacted with an antibody against the LS polypeptide. Amino acid sequences of these polypeptides were determined and compared with that deduced from the LS gene (rbcL) screened from the chloroplast DNA library of B. maxima. The N-terminal sequence of the LS peptide was not post-translationally processed and was almost identical with those of the polypept

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Matoba, S., J. Fukayama, R. A. Wing, and D. M. Ogrydziak. "Intracellular precursors and secretion of alkaline extracellular protease of Yarrowia lipolytica." Molecular and Cellular Biology 8, no. 11 (1988): 4904–16. http://dx.doi.org/10.1128/mcb.8.11.4904-4916.1988.

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Processing and secretion of the alkaline extracellular protease (AEP) from the yeast Yarrowia lipolytica was studied by pulse-chase and immunoprecipitation experiments. Over half of newly synthesized AEP was secreted by 6 min. Over 99% of AEP activity which was external to the cytoplasmic membrane was located in the supernatant medium. Polypeptides of 55, 52, 44, 36, and 32 kilodaltons (55K, 52K, 44K, 36K, and 32K polypeptides) were immunoprecipitated from [3H]leucine-labeled cell extracts by rabbit antibodies raised against mature, secreted AEP (32K polypeptide). Experiments with tunicamycin

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Matoba, S., J. Fukayama, R. A. Wing, and D. M. Ogrydziak. "Intracellular precursors and secretion of alkaline extracellular protease of Yarrowia lipolytica." Molecular and Cellular Biology 8, no. 11 (1988): 4904–16. http://dx.doi.org/10.1128/mcb.8.11.4904.

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Processing and secretion of the alkaline extracellular protease (AEP) from the yeast Yarrowia lipolytica was studied by pulse-chase and immunoprecipitation experiments. Over half of newly synthesized AEP was secreted by 6 min. Over 99% of AEP activity which was external to the cytoplasmic membrane was located in the supernatant medium. Polypeptides of 55, 52, 44, 36, and 32 kilodaltons (55K, 52K, 44K, 36K, and 32K polypeptides) were immunoprecipitated from [3H]leucine-labeled cell extracts by rabbit antibodies raised against mature, secreted AEP (32K polypeptide). Experiments with tunicamycin

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Gonçalves, Paloma, Francisco Martin, Patricia Borges, Maria Espirito Santo, Nuno Taveira, and José Marcelino. "PO 8597 NEUTRALISING AND NON-NEUTRALISING ANTIBODIES RESPONSE IN HIV-1-INFECTED INDIVIDUALS FROM MOZAMBIQUE." BMJ Global Health 4, Suppl 3 (2019): A61.2—A61. http://dx.doi.org/10.1136/bmjgh-2019-edc.161.

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BackgroundA vaccine that protects against the different HIV subtypes circulating around the world is essential to control and eliminate HIV infection. The immunogens are the key to develop an effective HIV vaccine. In this study, we characterised the antibody response against recombinant C2V3C3 polypeptides from several HIV-1 subtypes and evaluated the neutralising antibody response.MethodsPlasmas from HIV-1-infected individuals under treatment (n=39) and drugs-naïve individuals (n=8) were tested in an ELISA assay to determine the presence of antibodies against polypeptides from HIV-1 subtypes

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Asada, T., and H. Shibaoka. "Isolation of polypeptides with microtubule-translocating activity from phragmoplasts of tobacco BY-2 cells." Journal of Cell Science 107, no. 8 (1994): 2249–57. http://dx.doi.org/10.1242/jcs.107.8.2249.

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As part of our efforts to understand the molecular basis of the microtubule-associated motility that is involved in cytokinesis in higher plant cells, an attempt was made to identify proteins with the ability to translocate microtubules in an extract from isolated phragmoplasts. Homogenization of isolated phragmoplasts in a solution that contained MgATP, MgGTP and a high concentration of NaCl resulted in the release from phragmoplasts of factors with ATPase and GTPase activity that were stimulated by microtubules. A protein fraction with microtubule-dependent ATPase and GTPase activity caused

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Schlauder, G. G., M. P. Bell, B. N. Beck, A. Nilson, and D. J. McKean. "The structure-function relationship of I-A molecules: a biochemical analysis of I-A polypeptides from mutant antigen-presenting cells and evidence of preferential association of allelic forms." Journal of Immunology 135, no. 3 (1985): 1945–54. http://dx.doi.org/10.4049/jimmunol.135.3.1945.

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Abstract Chemically induced mutants of an I-Ak,d-expressing, antigen-presenting B cell-B lymphoma hybridoma have recently been generated by immunoselection in vitro with I-Ak-specific monoclonal antibodies, and were found to possess alterations in some of the I-Ak region-dependent functions. The mutants were categorized as alpha-polypeptide mutants or beta-polypeptide mutants on the basis of the patterns of reactivity with anti I-Ak alpha and anti I-Ak beta monoclonal antibodies. To delineate the structural alterations underlying the differences in serologic and functional properties of these

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Lee, DaeYong, N. Rejinold, Seong Jeong, and Yeu-Chun Kim. "Stimuli-Responsive Polypeptides for Biomedical Applications." Polymers 10, no. 8 (2018): 830. http://dx.doi.org/10.3390/polym10080830.

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Stimuli-responsive polypeptides have gained attention because desirable bioactive properties can be easily imparted to them while keeping their biocompatibility and biodegradability intact. In this review, we summarize the most recent advances in various stimuli-responsive polypeptides (pH, reduction, oxidation, glucose, adenosine triphosphate (ATP), and enzyme) over the past five years. Various synthetic strategies exploited for advanced polypeptide-based materials are introduced, and their applicability in biomedical fields is discussed. The recent polypeptides imparted with new stimuli-resp

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Nybroe, O., M. Albrechtsen, J. Dahlin, et al. "Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C." Journal of Cell Biology 101, no. 6 (1985): 2310–15. http://dx.doi.org/10.1083/jcb.101.6.2310.

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The biosynthesis of the neural cell adhesion molecule (N-CAM) was studied in primary cultures of rat cerebral glial cells, cerebellar granule neurons, and skeletal muscle cells. The three cell types produced different N-CAM polypeptide patterns. Glial cells synthesized a 135,000 Mr polypeptide B and a 115,000 Mr polypeptide C, whereas neurons expressed a 200,000 Mr polypeptide A as well as polypeptide B. Skeletal muscle cells produced polypeptide B. The polypeptides synthesized by the three cell types were immunochemically identical. The membrane association of polypeptide C was investigated w

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Newsted, W. Jay, and N. P. A. Huner. "Major sclerotial polypeptides of psychrophilic fungi: temperature regulation of in vivo synthesis in vegetative hyphae." Canadian Journal of Botany 66, no. 9 (1988): 1755–61. http://dx.doi.org/10.1139/b88-241.

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Western blot analysis of the major sclerotial polypeptides of the psychrophilic species Myriosclerotinia borealis (W51) and Coprinus psychromorbidus (LRS131) indicated that these polypeptides were not present in vegetative hyphae during growth at permissive temperature (5 °C), but significant accumulations were observed in hyphae upon prolonged exposure to nonpermissive temperature (25 °C). In contrast, low levels of sclerotial polypeptides were detected in the vegetative hyphae of Typhula incarnata (W29) and Typhula idahoensis (W21). We show, for the first time, that the in vivo synthesis of

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Bissig, Iwan, René A. Brunisholz, Franz Suter, Richard J. Cogdell, and Herbert Zuber. "The complete amino acid sequences of the b 800—850 antenna polypeptides from rhodopseudomonas acidophila strain 7750." Zeitschrift für Naturforschung C 43, no. 1-2 (1988): 77–83. http://dx.doi.org/10.1515/znc-1988-1-216.

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Spectrally pure B 800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (α, β) have been isolated by organic solvent extraction of the lyophilised B 800-850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degradation. B 800-850-a consists of 53 amino acids and is 45

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Ashcom, J. D., S. E. Tiller, K. Dickerson, J. L. Cravens, W. S. Argraves, and D. K. Strickland. "The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin." Journal of Cell Biology 110, no. 4 (1990): 1041–48. http://dx.doi.org/10.1083/jcb.110.4.1041.

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Ligand affinity chromatography was used to purify a cell surface alpha 2-macroglobulin (alpha 2M) receptor. Detergent extracts of human placenta were applied to an affinity matrix consisting of alpha 2M, previously reacted with methylamine, coupled to Sepharose. Elution with EDTA specifically released polypeptides with apparent molecular masses of 420 and 39 kD. In some preparations, small amounts of a 90-kD polypeptide were observed. The 420- and 39-kD polypeptides appear specific for the forms of alpha 2M activated by reaction with proteinases or methylamine and do not bind to an affinity ma

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Delgadoa, Fernando, Monica Brito, Ilona I. Concha, Ricardo Schroeder, and Luis O. Burzio. "Nuclear Sm antigens in the sperm of different organisms." Zygote 2, no. 3 (1994): 227–35. http://dx.doi.org/10.1017/s0967199400002021.

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SummaryImmunoblot analysis of sperm protein from several species revealed the presence of polypeptides recognised by anti-Sm sera obtained from patients with systemic lupus erythematosus. Immunoreactive polypeptides in human, bull, mouse and rat sperm were identified as protein B', B and D as compared with the Sm polypeptides of HeLa cells. In the sperm of rooster, the teleost fish Cyprinus carpio and the mussel Choromytilus chorus, the immunoreactive polypeptide profile was more complex. To ascertain the sperm origin of the Sm antigens, immunolocalisation with anti-Sm serum was carried out. T

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Alarcón, V. B., M. F. Filosa, and J. H. Youson. "Keratin polypeptides in the epidermis of the larval (ammocoete) sea lamprey, Petromyzon marinus L., show a cell type-specific immunolocalization." Canadian Journal of Zoology 72, no. 1 (1994): 190–94. http://dx.doi.org/10.1139/z94-025.

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Using immunofluorescent staining, the localization of keratin polypeptides in the epidermis of the larval (ammocoete) sea lamprey, Petromyzon marinus L., is described. Immunostaining with monoclonal antibodies against human keratin polypeptides showed that immunoreactivity was distributed in a cell type-specific pattern among the epidermal cells of ammocoete skin: immunoreactivity for keratin polypeptides Nos. 7 and 18 was prominent in skein and granular cells, respectively, while that for keratin polypeptide No. 19 was in cytoplasmic regions near the plasma membrane of both specialized (skein

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Giménez, Luis G., Jose Rojas, Almudena Rojas, Joaquín Mendoza, and Ana G. Camacho. "Development of an Enzyme-Linked Immunosorbent Assay-Based Test with a Cocktail of Nucleocapsid and Spike Proteins for Detection of Severe Acute Respiratory Syndrome-Associated Coronavirus-Specific Antibody." Clinical and Vaccine Immunology 16, no. 2 (2008): 241–45. http://dx.doi.org/10.1128/cvi.00252-08.

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ABSTRACT A new enzyme-linked immunosorbent assay (ELISA)-based immunoglobulin G (IgG)-plus-IgM antibody detection test for severe acute respiratory syndrome (SARS) has been developed by using a cocktail of four recombinant polypeptides as the antigen. These recombinant fragments were designed as parts of two different structural proteins from SARS-associated coronavirus (SARS-CoV). One recombinant polypeptide, S251-683, was designed as part of the spike glycoprotein, and the other three polypeptides comprised almost the whole nucleocapsid protein, avoiding the last 25 C-terminal amino acids. I

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