| Regeneration of immunosorbent surfaces used in clinical, industrial and environmental biosensors. Role of covalent and non-covalent interactions. | |
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MedLine Citation:
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PMID: 2197334 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The durability and regeneration of antibodies immobilized to commercial immunosorbents were investigated by monitoring Ag-Ab dissociation. Solutions consisting of 0.01 M hydrochloric acid (HCl), 10% propionic acid, 50% ethylene glycol and 10% SDS in 6 M urea were used in the evaluation of antigen dissociation from antibody covalently immobilized to glass and polystyrene beads, microtiter plates and Immobilon filters. RAH-IgG, used as a model antibody, bound strongly to all covalent surfaces. However, on adsorption to Nunc-1 microtiter plates, 25-60% of RAH-IgG was removed by all dissociating solutions. Covalent binding to Sanger beads was weakest relative to other covalent surfaces, exhibiting 30% and 65% detachment with ethylene glycol and SDS in urea, respectively. Although all four solutions dissociated antigen from surface-bound antibody, HCl and propionic acid were more effective on most surfaces. The antibody remained functional following antigen dissociation and reassociated to nearly 100% on all surfaces except Sanger beads and Nunc-1 microtiter plates. This study was initiated to evaluate regeneration and reuse of microelisa plates and emerging biosensors as a means of reducing routine laboratory analysis costs. Data are presented to demonstrate the reusability of microtiter plates in ELISAs following antigen dissociation from covalently bound antibody. |
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Authors:
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G C Blanchard; C G Taylor; B R Busey; M L Williamson |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Journal of immunological methods Volume: 130 ISSN: 0022-1759 ISO Abbreviation: J. Immunol. Methods Publication Date: 1990 Jul |
Date Detail:
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Created Date: 1990-08-24 Completed Date: 1990-08-24 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 1305440 Medline TA: J Immunol Methods Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 263-75 Citation Subset: IM |
Affiliation:
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Veterans Administration Medical Center, Boston, MA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Antigen-Antibody Complex* Biosensing Techniques* Enzyme-Linked Immunosorbent Assay Horseradish Peroxidase Immunoglobulin G Immunosorbent Techniques* Solvents Sulfuric Acids |
| Chemical | |
Reg. No./Substance:
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0/Antigen-Antibody Complex; 0/Immunoglobulin G; 0/Solvents; 0/Sulfuric Acids; 7664-93-9/sulfuric acid; EC 1.11.1.-/Horseradish Peroxidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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