The variable domain glycosylation in a monoclonal antibody specific to GnRH modulates antigen binding

Khurana, Sumit ; Raghunathan, Vidya ; Salunke, Dinakar M. (1997) The variable domain glycosylation in a monoclonal antibody specific to GnRH modulates antigen binding Biochemical and Biophysical Research Communications, 234 (2). pp. 465-469. ISSN 0006-291X

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1006/bbrc.1997.5929

Abstract

Functionally important glycosylation has been identified in the antigen binding domain of an anti-GnRH monoclonal antibody. Presence of mannose and sialic acid residues is revealed from con A immunoblots and positive staining with a sialic acid detection kit, respectively. Desialylation of the antibody reduces GnRH binding, suggesting the role of terminal sialic acid residues in modulating antigen binding. The crystal structure of the Fab fragment shows electron density adjacent to the antigen binding site which may be attributed to the covalently attached carbohydrate moiety. Thus, the presence of sialic acid containing mannose-rich carbohydrate moiety near the antigen binding site of a monoclonal antibody Fab fragment is relevant for defining antibody specificity.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:52502
Deposited On:04 Aug 2011 08:00
Last Modified:04 Aug 2011 08:00

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