Reports

Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes

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Science  23 May 1986:
Vol. 232, Issue 4753, pp. 1001-1004
DOI: 10.1126/science.2422757

Abstract

A monoclonal antibody bound to a protein antigen decreases the rate of proteolytic cleavage of the antigen, having the greatest effect on those regions involved in antibody contact. Thus, an epitope can be identified by the ability of the antibody to protect one region of the antigen more than others from proteolysis. By means of this approach, two distinct epitopes, both conformationally well-ordered, were characterized on horse cytochrome c.

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