|
Abstract:
Methods for pretreatment and rejuvenation of preimmobilized globular proteins used in immunodiagnostics were investigated using reagents routinely used in ELISA's. Rabbit and goat gamma globulins, functioning as antigens, and antibodies on non-covalent, and covalent solid surfaces, were monitored for detergent mediated desorption, denaturation, non-specific binding and altered antigenicity. The results from fourteen commercially supplied polyvinyl- and polystyrene-derivatized microtiter plates coated with antibody or antigenic lgG were compared with commercial microtiter diagnostic plates with preimmobilized lgG. Wash solutions had no effect on immobilized gamma globulins when the solid phase protein functioned as an antibody on covalent or noncovalent surfaces. In addition to tween 20 removing up to 50% of noncovalently bound protein additional binding sites are apparently exposed on solid phase antigens, evident by an increase in signal, which cannot be explained by nonspecific binding. However, no increase in signal was evident when antigen was preimmobilized covalently. The role of tween 20 and other reagent components in ELISA-based assays are explored. The screening of noncovalent preimmobilized antigen coated surfaces prior to use for deteraent mediated enhancement is suggested.
| Description: |
Final rept. Sep 89-Sep 91 |
| Pages: |
20 |
| Report Date: |
OCT 94 |
| Contract Number: |
DAAA15-89-C-0511 |
| Report Number: |
A925982 |
Report Unavailable |
| This title is unavailable from Storming Media. We do not know when it might be available, if at all. We list the report on our site for bibliographic completeness, to help our users know what other work has been performed in this field. Please note that as with all titles on this site, we do not have contact information for any of the authors. Nor can we give any suggestions on how one might obtain this report. |
|
|
|
|
|
Keywords relating to this report:
Email This Abstract
