کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9902227 | 1545795 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay
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کلمات کلیدی
AGMkoffNSBKinExAKinetic exclusion assay - آزمون خروج جنبشیnon-specific binding - اتصال غیر اختصاصیELISA - تست الیزاEnzyme-linked immunosorbent assay - تست الیزاequilibrium dissociation constant - تعادل تعادل ثابتassociation rate constant - ثابت نرخ ارتباطdissociation rate constant - ثابت نرخ انحلالkon - می تواندAffinity constant - وابستگی ثابتAntibody - پادتَن یا آنتیبادیCell surface receptor - گیرنده سطح سلولInsulin-like growth factor receptor - گیرنده فاکتور رشد مانند انسولین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوتکنولوژی یا زیستفناوری
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay](/preview/png/9902227.png)
چکیده انگلیسی
Measuring a protein-ligand interaction in solution, away from the ligand's cellular environment, may not provide an affinity value applicable in vivo. Here, we present a simple, accurate and highly sensitive method for determining the antibody affinity to cell surface receptor, hIGFR, and compare this data to affinity determined for the soluble receptor. Measurements were performed on both full-length bivalent IgG and the monovalent Fab fragments to assess possible differences in apparent affinity introduced by avidity of the bivalent IgG. Affinities determined for soluble hIGFR were 4 Ã 10â 12 M for the bivalent IgG and monovalent Fab. Comparable affinities of 6 Ã 10â 12 M and 1 Ã 10â 11 M for the bivalent IgG and Fab, respectively, were also determined for full-length hIGFR on cell surface. The method described allows estimation of reactant concentrations (anti-IGFR antibody) relative to one known reference concentration (the concentration of soluble hIGFR in our case) allowing us to estimate the average receptor density on the cell surface. Taken together, we believe these data can provide valuable insight into antibody behavior in vivo, especially in the case of insoluble or difficult to purify transmembrane receptors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Immunological Methods - Volume 304, Issues 1â2, September 2005, Pages 1-14
Journal: Journal of Immunological Methods - Volume 304, Issues 1â2, September 2005, Pages 1-14
نویسندگان
Lei Xie, R. Mark Jones, Thomas R. Glass, Ryman Navoa, Yan Wang, Michael J. Grace,