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Stability of assembled epitopes on human chorionic gonadotropin to covalent modifications

Venkatesh, N and Murthy, GS (1997) Stability of assembled epitopes on human chorionic gonadotropin to covalent modifications. In: Biochemistry and Molecular Biology International, 42 (4). pp. 853-863.

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Official URL: http://www3.interscience.wiley.com/journal/1178885...

Abstract

A measure of stability of a given epitope is an important parameter in the exploration of the utility of a desired MAb. It defines the conditions necessary for using MAbs as an investigative tool in several research methodologies and therapeutic protocols. Despite these obvious interests the lack of simple and rapid assay systems for quantitating MAb-Ag interactions has largely hampered these studies. A single step MAb-Solid Phase Radioimmunoassay (SS-SPRIA), is described which eliminates errors that may arise with multistep sandwich assays. SS-SPRIA has been used to demonstrate the differential stability of the assembled epitopes on gonadotropins. Differential stability towards specific reagents can be exploited to identify aminoacid residues at the epitopic site. Inactivation of an epitopic region is indicative of the presence of the group modified, provided conformational relaxations are not induced due to modifications at distant sites. Here we provide evidence to validate these conclusions.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Academic Press Aust.
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)
Date Deposited: 19 Jan 2010 06:31
Last Modified: 19 Sep 2010 05:52
URI: http://eprints.iisc.ernet.in/id/eprint/24868

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