Highly sensitive enzyme immunoassay of rabbit (anti-human IgG) IgG using human IgG-β-D-galactosidase conjugate
نویسندگان
چکیده
منابع مشابه
Glycation of Human IgG Induces Structural Alterations Leading to Changes in its Interaction with Anti-IgG
Background: Glycation of proteins is a non-enzymatic spontaneous process that occurs in diabetes mellitus and aging, altering the structure and function of proteins. IgG undergoes glycation leading to changes in its reactivity to antigen and fixation of complement. Objective: This study aimed at revealing the effect of glycation on the interaction of IgG with anti-IgG using electroimmunoassay...
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AIMS To review the performance of the Venereal Diseases Research Laboratory (VDRL) test and the Treponema pallidum haemagglutination assay (TPHA) as a combined screen for syphilis to provide a baseline for assessing screening by anti-treponemal IGG EIA. METHODS Between 1980 and 1987 all serum samples were screened by both VDRL and TPHA tests. The FTA-ABS test was also used in suspected early ...
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Interactions between antibody and antigen molecules play essential roles in biological recognition processes as well as medical diagnosis. Therefore, an understanding of the underlying mechanism of antibody-antigen interactions at the single molecular level would be beneficial. In the present study, human immunoglobulin (IgG) tethered cantilevers and rat anti-human IgG functionalized gold surfa...
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Background: The affinity of an antibody to its antigen is a crucial parameter in its biological activity and performance of an immunoassay such as ELISA. Affinity of most IgG specific MAbs are often determined by methods which require labeling of either antigen or antibody, and are sometimes difficult to control, do not always lead to the expected signal and often result in immunological modifi...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1980
ISSN: 0014-5793
DOI: 10.1016/0014-5793(80)80825-8