Relevant bibliographies by topics / Immunoassay Enzyme-linked immunosorbent assay

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Immunoassay Enzyme-linked immunosorbent assay'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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Gan, Stephanie D., and Kruti R. Patel. "Enzyme Immunoassay and Enzyme-Linked Immunosorbent Assay." Journal of Investigative Dermatology 133, no. 9 (2013): 1–3. http://dx.doi.org/10.1038/jid.2013.287.

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Lequin, Rudolf M. "Enzyme Immunoassay (EIA)/Enzyme-Linked Immunosorbent Assay (ELISA)." Clinical Chemistry 51, no. 12 (2005): 2415–18. http://dx.doi.org/10.1373/clinchem.2005.051532.

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Abstract This brief note addresses the historical background of the invention of the enzyme immunoassay (EIA) and enzyme-linked immunosorbent assay (ELISA). These assays were developed independently and simultaneously by the research group of Peter Perlmann and Eva Engvall at Stockholm University in Sweden and by the research group of Anton Schuurs and Bauke van Weemen in The Netherlands. Today, fully automated instruments in medical laboratories around the world use the immunoassay principle with an enzyme as the reporter label for routine measurements of innumerable analytes in patient samples. The impact of EIA/ELISA is reflected in the overwhelmingly large number of times it has appeared as a keyword in the literature since the 1970s. Clinicians and their patients, medical laboratories, in vitro diagnostics manufacturers, and worldwide healthcare systems owe much to these four inventors.
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Dasgupta, Amitava, Edward Kang, Margaret Olsen, Jeffrey K. Actor, and Pradip Datta. "Interference of Asian, American, and Indian (Ashwagandha) Ginsengs in Serum Digoxin Measurements by a Fluorescence Polarization Immunoassay Can Be Minimized by Using a New Enzyme-Linked Chemiluminescent Immunosorbent or Turbidimetric Assay." Archives of Pathology & Laboratory Medicine 131, no. 4 (2007): 619–21. http://dx.doi.org/10.5858/2007-131-619-ioaaai.

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Abstract Context.—Ginsengs are widely used by the general population. These herbs interfere with serum digoxin measurement using the fluorescence polarization immunoassay. Objective.—To assess potential interference of different ginsengs (Asian, American, and Indian, also known as Ashwagandha) in vitro and in vivo in a mouse model by using a new enzyme-linked chemiluminescent immunosorbent digoxin assay and an existing turbidimetric assay. Comparisons were made with the fluorescence polarization immunoassay. Design.—Aliquots of drug-free serum pools were supplemented with ginseng and apparent digoxin concentrations were measured using enzyme-linked chemiluminescent immunosorbent digoxin assay, turbidimetric assay, and fluorescence polarization immunoassay digoxin assays. Mice were fed with different ginseng preparations and apparent digoxin concentrations were measured 1 and 3 hours later. In a separate experiment, aliquots of serum digoxin pools were further supplemented with ginsengs and the serum digoxin concentrations were measured again. Results.—A significant apparent digoxin concentration was observed both in vitro and in vivo using the fluorescence polarization immunoassay, but no apparent digoxin concentration was observed using enzyme-linked chemiluminescent immunosorbent digoxin assay and turbidimetric assay. No interference was observed with enzyme-linked chemiluminescent immunosorbent digoxin assay and turbidimetric assay when digoxin serum pools were further supplemented with various ginsengs. Conclusions.—It was concluded that both enzyme-linked chemiluminescent immunosorbent and turbidimetric digoxin assays are free from ginseng interferences.
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Sathe, Manisha, Shruti Srivastava, Sumit Agrawal, and Ramrao Ghorpade. "Effect of Spacer and the Enzyme-Linked Immunosorbent Assay." Defence Science Journal 66, no. 5 (2016): 471. http://dx.doi.org/10.14429/dsj.66.10700.

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The effect of spacers and the enzyme-linked immunosorbent assay (ELISA) formats on the functional parameters of assays such as lower detection limit, inhibitory concentration at 50 per cent (IC50), and specificity were studied. Enzyme conjugates having hydrophobic and hydrophilic spacers were prepared using O-isopropyl methylphosphonic acid (IMPA) and horseradish peroxidase (HRP) as an enzyme label. Comparison was made with reference to enzyme conjugate without any spacer. The present investigation revealed that the presence of a hydrophilic spacer in the enzyme conjugate significantly improves the sensitivity of assays. An enhanced IC50 value achieved was 0.01 μg mL−1 for free antigen detection by direct immunoassay using hydrophilic spacers and precoating of ELISA plates by secondary antibody. The use of a hydrophilic spacer might have helped in projecting the hapten in the aqueous phase, leading to enhanced antibody binding signal and improved sensitivity of the assay.
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Vítková, M., Z. Macková, R. Koblovská, and O. Lapčík. "Enzyme-linked immunosorbent assay for the determination of isoflavones in alimentary important plants." Czech Journal of Food Sciences 22, SI - Chem. Reactions in Foods V (2004): S199—S202. http://dx.doi.org/10.17221/10659-cjfs.

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The development of polyclonal antibody-based enzyme-linked immunosorbent assays (ELISA) for the determination of individual isoflavones, i.e. daidzein, genistein and biochanin and their homologues, is presented in this work. Isoflavone conjugates with bovine serum albumin were used as immunogens, coupled at the position C 7 and C 4’ via a carboxy methyl spacer. The developed ELISAs are highly specific, I<sub>50</sub> values of the standard curves range between 0.3–1.2 ng/ml. The cross reactivities to other isoflavones are in acceptable range and the interference of non-isoflavonoid molecules is negligible. The immunoassays have been used for monitoring of changes in isoflavone levels in alimentary important plants, such as Medicago sativa, during germination; and during different vegetation stages of the Rutaceae family plants.
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Du, Pengfei, Maojun Jin, Lihua Yang, et al. "A rapid immunomagnetic-bead-based immunoassay for triazophos analysis." RSC Advances 5, no. 99 (2015): 81046–51. http://dx.doi.org/10.1039/c5ra15106f.

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Heinegård, D., A. Björne-Persson, L. Cöster, et al. "The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroups." Biochemical Journal 230, no. 1 (1985): 181–94. http://dx.doi.org/10.1042/bj2300181.

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Large and small proteoglycans were separately isolated from a number of connective tissues and compared to determine the extent of structural similarity. This was studied by enzyme-linked immunosorbent assays and by the peptide patterns obtained when 125I-labelled proteoglycans were digested with trypsin. All the large proteoglycans, i.e. from tendon, sclera, cartilage and aorta, appear to contain the structure typical for the hyaluronic acid-binding region, both shown by enzyme-linked immunosorbent assay and by content of peptides unique for this region. These proteoglycans also share other structural features of the protein core, as indicated by immunological cross-reactivity and similar peptide patterns. The large proteoglycans from aorta in addition show the presence of unique structures both upon immunoassay and with regard to peptide pattern. Among the small proteoglycans two groups can be identified, although amino acid composition and protein core sizes are grossly similar. One group consists of the small proteoglycans from aorta and cartilage having similar peptide maps and showing immunological cross-reactivity in enzyme-linked immunosorbent assay. The other distinctly different group consists of the small proteoglycans from bone, cornea, sclera and tendon, which among them show identity in enzyme-linked immunosorbent assay and similar peptide patterns. Proteoglycans from the two groups, however, show partial immunological cross-reactivity.
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Radhakrishnan, Jeejabai, Rovi Origenes, Gina Littlejohn, et al. "Plasma Cytochrome c Detection Using a Highly Sensitive Electrochemiluminescence Enzyme-Linked Immunosorbent Assay." Biomarker Insights 12 (January 1, 2017): 117727191774697. http://dx.doi.org/10.1177/1177271917746972.

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Background: Cytochrome c is an intermembrane mitochondrial protein that is released to the bloodstream following mitochondrial injury. Methods and results: We developed an electrochemiluminescence immunoassay to measure cytochrome c in human and rat plasma, which showed high sensitivity with broad dynamic range (2-1200 ng/mL in humans and 5-500 ng/mL in rat) and high assay reproducibility (inter-assay coefficient <6% in humans and <10% in rat). In patients after blunt trauma, plasma cytochrome c directly correlated with injury severity. In rats after cardiac resuscitation, plasma cytochrome c inversely correlated with survival and responsiveness to mitochondrial protective interventions. Conclusions: The cytochrome c assays herein presented have high sensitivity, wide dynamic range, and high reproducibility well suited for biomarker of mitochondrial injury.
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Ehm, M., and A. Kappel. "Immunoassays for diagnosis of coagulation disorders." Hämostaseologie 30, no. 04 (2010): 194–201. http://dx.doi.org/10.1055/s-0037-1619055.

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SummaryImmunoassays play a pivotal role in the clinical laboratory. In the coagulation section of the laboratory, they are used as an aid for diagnosis of deep vein thrombosis or pulmonary embolism, thrombophilia screening, or detection of coagulation factor deficiencies, respectively. Enzyme-linked immunosorbent assay (ELISA) and latex agglutination immunoassay technologies are currently most widely used, while Luminescent Oxygen Channeling Immuno - assay (LOCI®) and other chemiluminescencebased immunoassays are emerging technologies for the coagulation laboratory. However, not all immunoassay technologies employed are compatible with the workflow requirements of the coagulation laboratory, and, not all technologies are suitable for detection or quantification of every marker.This review focuses on technical and performance aspects of those immunoassay technologies that are most widely used in the coagulation laboratory, and provides a description of markers that are typically tested by immunoassays.
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van der Ende, A., R. W. M. van der Hulst, P. Roorda, G. N. J. Tytgat, and J. Dankert. "Evaluation of Three Commercial Serological Tests with Different Methodologies To Assess Helicobacter pyloriInfection." Journal of Clinical Microbiology 37, no. 12 (1999): 4150–52. http://dx.doi.org/10.1128/jcm.37.12.4150-4152.1999.

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The sera of 142 Helicobacter pylori-positive and 32H. pylori-negative patients were assessed by a desktop test (QuickVue), an enzyme-linked immunosorbent assay (ELISA) (HM-CAP), and a solid-phase, two-step chemiluminescent enzyme immunoassay (Immulite). These tests yielded sensitivities of 97, 97, and 91% and specificities of 97, 94, and 100%, respectively. In conclusion, the desktop test and the ELISA are more sensitive than the chemiluminescent enzyme immunoassay (P < 0.05). The chemiluminescent enzyme immunoassay has the advantage that it is fully automated.
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Dissertations / Theses on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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Carroll, Andrea D. "Development of bead injection methodology for immunoassays /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8599.

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Orchard, Robert Graham. "A flow-through enzyme-linked immunoassay for progesterone." The University of Waikato, 2007. http://hdl.handle.net/10289/2277.

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Bovine reproductive performance is one of the most important factors influencing dairy farm profitability. Present-day techniques for oestrus- and pregnancy-detection are unreliable and labour-intensive. Although measuring milk-progesterone at regular intervals allows the fertility status of a cow to be determined reliably, the labour cost of collecting and analysing samples is prohibitive. This project aimed to develop a progesterone sensing system that could be automated and integrated with the milking unit, thus minimising labour costs. The proposed system involved mixing the milk sample with an enzyme-antibody conjugate and then passing the sample through a column containing immobilised progesterone. Any progesterone in the milk would inhibit conjugate binding to the column. An enzyme substrate would then flow through the column and bound conjugate would be detected as a colour change at the column's outlet. Periodate-coupling was used to attach horseradish peroxidase enzyme to anti-progesterone antibody, and progesterone-3-carboxymethyloxime was immobilised on the polystyrene bead surface using amine-coupling. Both techniques are widely used. Initial experiments attempted to verify the success of these two reactions simultaneously, whereas later experiments focused on the bead-coating. Beads were suspended in a specially-constructed syringe and the antibody activity of the eluted solution was measured by SPR. However, a combination of non-specific binding and antibody stability and activity issues meant neither reaction was conclusively verified. Many trials were done to investigate how to overcome the problems encountered but a suitable, workable procedure was not developed. Despite poor progress, the problems encountered did not undermine the project's potential. There remains optimism of developing an on-line method if research were to continue.
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Campbell, Charles Nelson. "Separationless immunoassay and DNA sensing using wired enzyme based amperometric affinity electrodes /." Digital version:, 2000. http://wwwlib.umi.com/cr/utexas/fullcit?p9992761.

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de, Alwis Wathuthanthirige Uditha. "Analytical applications of chemically modified antibodies." Diss., The University of Arizona, 1988. http://hdl.handle.net/10150/184601.

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The components involved in an immunoassay were investigated in order to improve the detection limits of the ELISA and to make the assay adaptable to a flow injection analysis (FIA) configuration. The goal being the total automation of the ELISA procedure which is long, tedious and has high standard deviation. The antibody purification and cleavage methods were studied with special emphasis on obtaining products with highest immunological activity. The antibody-enzyme coupling reactions using homobifunctional reagents and heterobifunctional reagents were studied in order to attempt the preparation of highly characterized reagents. The fragments of IgG were coupled to polymeric supports via the hinge thiol groups to retain the maximum immunological activity. This method was found to be superior to those methods involving coupling via amino group. These reagents were used in the development of a sandwich ELISA for bovine IgG. The range of assay was in the 20-1000 femtomole range with a linear dynamic range of 2 orders of magnitude and an accuracy of 2-5%. A competitive ELISA based on the use of immobilized anti-human IgG Fab' fragments was developed. The linear dynamic range for this assay was found to be less than one order of magnitude. The detection limit was in the low picomole range with an accuracy of 2-5%. Based on the principle used in the two assays an enzyme immobilization scheme was developed for the reversible immobilization of these enzymes. Which was subsequently utilized in the determination of substrate in the picomole range in a reagent less FIA technique. The goals of this research project were realized in that the FIA system utilized in this work was capable of carrying out totally automated ELISA assays with an accuracy far surpassing the conventional plate ELISA assays.
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Lövgren, Ulf. "Enzyme immunoassay in combination with liquid chromatography for sensitive and selective determination of drugs in biosamples." Lund : Dept. of Analytical Chemistry, Lund University, 1997. http://books.google.com/books?id=Ju1qAAAAMAAJ.

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Kiote-Schmidt, Chrissoula. "Etablierung eines kompetitiven enzymgekoppelten Immunoassays zum Nachweis eines kleinen Peptids in Serum- und Liquorproben." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:289-vts-59192.

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Booth, Ronald A. Carleton University Dissertation Biology. "Development of cloth-enzyme immunoassays for the detection of E. coli O157 and verotoxin." Ottawa, 1996.

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Moberg, Ylva. "Evaluation of an equine-optimized enzyme-linked immunosorbent assay for the determination of serum insulin in canine and feline samples." Thesis, Uppsala universitet, Institutionen för kvinnors och barns hälsa, 2018. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-354036.

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Background: Insulin is an important hormone for glucose homeostasis. It is released from β-cells in the endocrine pancreas as a response to increased concentrations of plasma glucose. The major effect of insulin is the facilitation of cellular uptake and storage of glucose as glycogen. Insulinomas are tumours that produce excessive amounts of insulin resulting in hypoglycaemia. The condition has been observed in dogs and cats and is often malignant. One part of establishing the diagnosis is confirmation of elevated concentrations of insulin in a hypoglycaemic sample. Aim: The aim of this study was to evaluate if an equine-optimized insulin ELISA (Mercodia AB, Uppsala, Sweden) is useful for analysis of insulin in canine and feline serum samples when insulinoma is suspected. Material and methods: All samples were analysed with Equine insulin ELISA. Precision, linearity and effects of haemolysis were studied. The stability of insulin was evaluated after storage in 4°C, room temperature and after repeated freezing and thawing. A reference interval was constructed for both canine and feline samples. Results: Total precision expressed as CV was 4.4 – 18.9 %. The method was linear up to at least 100 mU/L for dogs and 15 mU/L for cats. Reference interval for cats was <11.6 mU/L, due to few healthy animals no reference interval for dogs could be established. Stability was acceptable for up to four days. No effects of haemolysis were detected. Conclusion: Mercodia Equine insulin ELISA is suitable for analysis of insulin in serum from dogs and cats when suspecting insulinoma.
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Hardy, Charles Thomas. "Evaluation and calibration of enzyme immunoassays for detecting antibody to the human immunodeficiency virus and other agents /." Thesis, Connect to this title online; UW restricted, 1993. http://hdl.handle.net/1773/9297.

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Kim, Sangkyung. "Redox cycling for an in-situ enzyme labeled immunoassay on interdigitated array electrodes." Diss., Available online, Georgia Institute of Technology, 2004:, 2004. http://etd.gatech.edu/theses/available/etd-08192004-105039/unrestricted/kim%5Fsangkyung%5F200412%5Fphd.pdf.

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Thesis (Ph. D.)--Biomedical Engineering, Georgia Institute of Technology, 2005.<br>Hesketh, Peter, Committee Chair ; Edmondson, Dale, Committee Member ; Frazier, Albert, Committee Member ; Hunt, William, Committee Member ; Janata, Jiri, Committee Member. Includes bibliographical references.
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Books on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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M, Cambra Alvarez, International Office of Epizootics, and Instituto Nacional de Investigaciones Agrarias., eds. Enzyme immunoassay techniques, ELISA, in animal and plant diseases. 2nd ed. Office international des épizooties, 1987.

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Koston, Suzanne C. Studies on the development of an Immunoassay to detect Neutrophil Collagenase (MMP-8). University College Dublin, 1997.

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International Symposium on "Advances in Immunoassays for Veterinary and Food Analysis" (2nd 1986 University of Surrey). Immunoassays for veterinary and food analysis. Elsevier Applied Science, 1988.

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Rothwell, E. An assessment of the value of IgM antibody to Hepatitis C virus using synthetic peptide enzyme immunoassays. University College Dublin, 1997.

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Handbook of ELISPOT: Methods and protocols. 2nd ed. Humana Press, 2012.

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Pape, Carsten. Melatoningehalt in marinen Makroalgen: Entwicklung und Validierung quantitativer Bestimmungen mittels HPLC und Enzym-gekoppeltem Immunoassay = Melatonin in marine macroalgae : development and validation of quantitative determinations by HPLC and enzyme-linked immunosorbent assay. Alfred-Wegener-Institut für Polar- und Meeresforschung, 2004.

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Hosseini, Samira, Patricia Vázquez-Villegas, Marco Rito-Palomares, and Sergio O. Martinez-Chapa. Enzyme-linked Immunosorbent Assay (ELISA). Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-6766-2.

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Enzyme immunoassays: From concept to product development. Chapman & Hall, 1996.

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The ELISA guidebook. 2nd ed. Humana Press, 2009.

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Calamel, Michel. E.L.I.S.A. standardised technique. Laboratoire national de pathologie des petits ruminants et des abeilles, 1988.

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Book chapters on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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Butler, J. E., J. H. Peterman, and T. E. Koertge. "The Amplified Enzyme-Linked Immunosorbent Assay (a-ELISA)." In Enzyme-Mediated Immunoassay. Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-5012-5_14.

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Alhabbab, Rowa Yousef. "Enzyme Immunoassay (EIAs) and Enzyme-Linked Immunosorbent Assay (ELISA)." In Techniques in Life Science and Biomedicine for the Non-Expert. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-77694-1_12.

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Smeenk, R. "DETECTION OF ANTIBODIES TO DNA BY ENZYME-LINKED IMMUNOSORBENT ASSAY (ELISA)." In Immunoassay Technology Vol. 2, edited by S. B. Pal. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110884692-007.

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Goldring, O. L. "DETERGENT SOLUBILISED ANTIGENS IN ENZYME IMMUNOASSAY WITH PARTICULAR REFERENCE TO ENZYME-LINKED IMMUNOSORBENT ASSAY (ELISA) SYSTEMS." In Immunoassay Technology Vol. 2, edited by S. B. Pal. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110884692-010.

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Schmitt, K., Erwin Märtlbauer, Ewald Usleber, R. Gessler, J. Lepschy, and David Abramson. "Detection of Acetylated Deoxynivalenol by Enzyme-Linked Immunosorbent Assay." In Immunoassays for Residue Analysis. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0621.ch023.

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Morsy, Mohamed A., Azza A. Ibrahim, and Mahmoud M. Hewedi. "Detection of Dieldrin by Enzyme-Linked Immunosorbent Assay in Some Dairy Products." In Immunoassays for Residue Analysis. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0621.ch013.

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Bushway, Rodney J., Titan S. Fan, Lynn E. Katz, et al. "Development of an Enzyme-Linked Immunosorbent Assay for Hexazinone and Its Application to Water." In Immunoassays for Residue Analysis. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0621.ch014.

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Morsy, Mohamed A., Azza A. Ibrahim, and Mahmoud M. Hewedi. "Detection of Pesticides in Human Milk Samples Collected in Egypt by Enzyme-Linked Immunosorbent Assay." In Immunoassays for Residue Analysis. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0621.ch012.

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Lopez-Avila, Viorica, Chatan Charan, and Jeanette Van Emon. "Supercritical Fluid Extraction—Enzyme-Linked Immunosorbent Assay Applications for Determination of Pesticides in Soil and Food." In Immunoassays for Residue Analysis. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0621.ch035.

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Töpfer, G. "Enzyme-linked Immunosorbent Assay." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1013.

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Conference papers on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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Sugihara, T., J. Takamatsu, T. Kamiya, H. Saito, K. Kimata, and K. Kato. "A SENSITIVE ENZYME-LINKED IMMUNOSORBENT ASSAY(ELISA) FOR SERUM LAMININ." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643554.

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Laminin, a large glycoprotein, is a major and specific component of basement membrane. There were little or no circulating laminin in normal persons, although some recent reports have showed increased values in various diseases(ex. diabetes mellitus and liver disease) by a radioimmunoassay(RIA) using laminin fragment. The minimum detectable sensitivity of RIA was reported to be 20 ng/ml of serum sample. We describe here a more sensitive immunoassay system, and also the concentrations of laminin in sera from healthy subjects and patients. A sandwich ELISA method for measurement of laminin was established by use of purified antibodies to mouse laminin. The assay system consisted of poly-stylene balls with immobilized antibody F(ab’)2 fragments and the same antibody Fab1 fragments labeled with β-D-galactosidase from E.Coli. The assay was highly sensitive and can detect as small as 0.5 ng/ml of serum laminin.Coefficients of variation in within-run and between-run precision studies for serum laminin were good. Serum laminin levels in healthy subjects of various ages ranged from 1.5 to 3.9 ng/ml(n=60). Fifty eight patient sera (collagen disease(n=18), hepatic disease(n=20), and renal disease (n=20)) were examined. Significant differences between the normal sera and 3 diseases sera were observed as shown belowIt is concluded that circulating laminin apparently exists in normal persons and there are higher laminin level in some diseases which appears to involve basement membrane-rich organ
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Tanaka, I., A. Yoshioka, T. Fujiwara, H. Nakai, and H. Fukui. "THE CHANGES OF FACTOR VIII ANTIGEN DURING THE COAGULATION PROCESS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644038.

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The changes of factor VIII (F. VIII) during blood coagulation process is still controversial. We analyzed the F. VIII antigen (F. VIII:Ag) at various intervals of in vitro blood clotting by immunoassays using polyclonal and different kinds of monoclonal antibodies to F. VIII.We used two immunoassays, an immunoradiometric assay (IRMA) and an enzyme-linked immunosorbent assay (ELISA). The IRMA was performed by the method of Peake et al. using high-titer allo-antibodies to F. VIII. The ELISA was performed by two-site solid phase system consisting of alloantibodies as the first and one of three kinds of monoclonal antibodies (NMC-VIII/1, -VIII/2 or C5*) as the second antibody. Using the immunoblotting technique, it had been shown that NMC-VIII/1 recognized the 80/79 kDa derived from C-terminus and both NMC-VIII/2 and C5 recognized 54 kDa derived from N-terminus.The mean levels of F. VIII:Ag in 20 normal plasmas and sera were 0.97±0.23 U/ml and 0.68±0.21 U/ml, respectively using the polyclonal IRMA. The mean levels of F. VIII:Ag in normal sera were 0.14±0.05 U/ml (NMC-VIII/1), 0.71±0.21 U/ml (NMC-VIII/2), and 0.012±0.02 U/ml (C5) using the monoclonal ELISAs. In the initial phase of whole blood coagulation in vitro, the increase of F. VIII: Ag was observed by the polyclonal IRMA as F. VIII:C assayed by a one-stage clotting method increased. On the other hand, the F. VIII:Ag assayed by NMC-VIII/1 or C5 monoclonal ELISA progressively decreased to the serum level within 30 min. The F. VIII:Ag by NMC-VIII/2 declined to the serum level at a slow rate. In order to study the influence of thrombin on F. VIIIrAg during blood clotting, a synthesized selective thrombin inhibitor (MD-805, Mitsubishi Chemical Ind.) was previously added to the whole blood tested. The changes of F. VIII:Ag with MD-805 by the monoclonal ELISAs were almost the same as those without MD-805.It is suggested that in the whole blood coagulation process the antigenicity of F. VIII molecule changes in the initial phase (within 30 min.), but that thrombin does not play the main role of the phenomenon in physiological concentration.*C5 was kindly supplied from Dr. C. Fulcher (Scripps Clinic and Research Foundation, USA)
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Ananda, Alfie Rizky, Donny Danudirdjo, Agung W. Setiawan, and Tati Latifah R. Mengko. "Development of LED Based Enzyme-Linked Immunosorbent Assay Reader." In 2021 IEEE 7th International Conference on Smart Instrumentation, Measurement and Applications (ICSIMA). IEEE, 2021. http://dx.doi.org/10.1109/icsima50015.2021.9526331.

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Ananda, Alfie Rizky, Donny Danudirdjo, Agung W. Setiawan, and Tati Latifah R. Mengko. "Development of Low Cost Enzyme-Linked Immunosorbent Assay Plate Reader." In 2019 International Symposium on Electronics and Smart Devices (ISESD). IEEE, 2019. http://dx.doi.org/10.1109/isesd.2019.8909658.

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Ishizawa, M., T. Azeta, H. Nose, Y. Ukita, and Y. Utsumi. "Three-dimensional lab-on-a-CD with enzyme-linked immunosorbent assay." In 2012 7th IEEE International Conference on Nano/Micro Engineered and Molecular Systems (NEMS). IEEE, 2012. http://dx.doi.org/10.1109/nems.2012.6196759.

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Berger, C., A. Pilch, J. Ruppert, FP Armbruster, and J. Stein. "An enzyme-linked immunosorbent assay for therapeutic drug monitoring of Golimumab." In Viszeralmedizin 2017. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1604810.

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Sasagawa, Kiyotaka, Soo Heyon Kim, Kazuya Miyazawa, et al. "Dual-mode lensless imaging device for digital enzyme linked immunosorbent assay." In SPIE BiOS, edited by Benjamin L. Miller, Philippe M. Fauchet, and Brian T. Cunningham. SPIE, 2014. http://dx.doi.org/10.1117/12.2039948.

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Váradi, K., J. Kárpáti, and S. Elödi. "ENZYME LINKED IMMUNOASSAY (ELISA) FOR FACTOR VIII ANTIGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644033.

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Abstract:
A two site ELISA test was developed for measuring factor VIII antigen (FVIIIsAg). The assay is based on two antibodies developed in a non-haemophilic and in a severe haemophilia-A patient, respectively. The IgG fraction prepared from the non-haemophilic plasma was used for coating, and the IgG isolated from the haemophilia-A plasma was labelled with horse-radish peroxidaseFVIII:Ag and FVIII activity was measured in 28 healthy blood donors and in 41 haemophilia-A patients. The normal range for FVIIIcAg was 40 - 180 %, the correlation coefficient between FVIII:Ag and FVIII activity assays was 0.8. The sensitivity of the assay ranges between 0.005 - 0.2 U/ml FVIII:Ag. In 18 cases of severe haemophilia-A FVIII:Ag was not detectable. In 3 out of 23 mild haemophilia-A cases FVIIIrAg was significantly higher, then FVIII activity, indicating CRM variants of the disease. Due to the high sensitivity of FVIII:Ag detection, the assay appears to be suitable for prenatal diagnosis
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Junwei, Liu, Jiang Jinqing, An Zhixing, Zhao Kun, Liu Xingyou, and Yao Sixin. "Preparation of a monoclonal antibody based sandwich enzyme-linked immunosorbent assay for Salmonella." In 2011 IEEE 3rd International Conference on Communication Software and Networks (ICCSN). IEEE, 2011. http://dx.doi.org/10.1109/iccsn.2011.6014317.

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Lee, Wen-Wai, Kuan-Ju Tseng, and Ju-Nan Kuo. "PDMS microlens fabricated for compact disk enzyme-linked immunosorbent assay (CD-ELISA) applications." In 2010 5th IEEE International Conference on Nano/Micro Engineered and Molecular Systems (NEMS 2010). IEEE, 2010. http://dx.doi.org/10.1109/nems.2010.5592184.

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Reports on the topic "Immunoassay Enzyme-linked immunosorbent assay"

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Occurrence and Distribution of Pesticides in the St. Lucie River Watershed, South-Central Florida, 2000-01, Based on Enzyme-Linked Immunosorbent Assay (ELISA) Screening. US Geological Survey, 2003. http://dx.doi.org/10.3133/wri024304.

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