HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Pressman, D. Articles by Grossberg, A. Search for Related Content PubMed PubMed Citation Articles by Pressman, D. Articles by Grossberg, A.

Retention of Rabbit Antibody Activity during Acetylation¹

From the Department of Biochemistry Research, Roswell Park Memorial Institute, Buffalo, New York

Abstract

Although acetylation destroys the ability of rabbit anti-BSA to form a precipitate with BSA it was found here that it still combines with BSA to form soluble complexes. The combination was studied by electrophoretic and ultracentrifugal methods. Acetylation of 96% of the amino groups of anti-BSA -globulin resulted in a preparation that could still form soluble complexes with BSA. Normal rabbit -globulin, however, when acetylated to 86% of its amino groups, did not form soluble complexes with BSA.

The failure of acetylated antibody to form a precipitate with its antigen is attributed to electrostatic repulsion effects between antibody molecules.

Footnotes

Supported in part by Grant E 2342 from the National Institute of Allergy and Infectious Disease.