Document Detail


Regeneration of immunosorbent surfaces used in clinical, industrial and environmental biosensors. Role of covalent and non-covalent interactions.
MedLine Citation:
PMID:  2197334     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
G C Blanchard; C G Taylor; B R Busey; M L Williamson
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of immunological methods     Volume:  130     ISSN:  0022-1759     ISO Abbreviation:  J. Immunol. Methods     Publication Date:  1990 Jul 
Date Detail:
Created Date:  1990-08-24     Completed Date:  1990-08-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  1305440     Medline TA:  J Immunol Methods     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  263-75     Citation Subset:  IM    
Affiliation:
Veterans Administration Medical Center, Boston, MA.
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MeSH Terms
Descriptor/Qualifier:
Antigen-Antibody Complex*
Biosensing Techniques*
Enzyme-Linked Immunosorbent Assay
Horseradish Peroxidase
Immunoglobulin G
Immunosorbent Techniques*
Solvents
Sulfuric Acids
Chemical
Reg. No./Substance:
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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