Abstract:
:Biologically active membrane proteins are difficult to isolate. Very often the isolated membrane proteins have low binding affinity or no biological integrity at all. Despite some success in isolation, one has to overcome the hurdles of obtaining sufficient quantity of the proteins and maintaining biological activity upon coating them on surfaces for developing an ELISA. Thus an alternative approach may be useful. The present study describes a quantification assay method for a therapeutic hmAb-1 (human monoclonal antibody-1) that recognizes a cell-surface protein employing an anti-ID (anti-idiotypic antibody) to hmAb-1 as a surrogate antigen in an immunoassay format using surface- plasmon-resonance technology. This assay is applicable for quantification of hmAb-1 in process streams, final drug-product quality control, as well as low-concentration drug substances in intravenous-solution bags. The surrogate nature of the anti-ID was confirmed by demonstrating that the anti-ID displaced the interaction between the hmAb-1 and its membrane antigen in a FACS titration test. The assay format involves first capturing hmAb-1 on the flow-cell surface, which then binds quantitatively to anti-ID in a mixture of increasing quantity of hmAb-1 in solution. An inverse dose-response relation between this anti-ID bound signal (or resonance units) and hmAb-1 concentration was established. The dose-response range of the calibration curve for hmAb-1 was between 20 and 300 ng/ml. The precision, accuracy and specificity of the assay are reported in the present paper.
journal_name
Biotechnol Appl Biochemjournal_title
Biotechnology and applied biochemistryauthors
Wong RB,Lee AH,Rangan VS,Cheng KCdoi
10.1042/BA20080072subject
Has Abstractpub_date
2009-05-01 00:00:00pages
51-61issue
Pt 1eissn
0885-4513issn
1470-8744pii
BA20080072journal_volume
53pub_type
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