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Antigenic Properties of Substituted Serum-Globulin

Felix Haurowitz, Kirkor arafian and Paula Schwerin

From the Institute of Biological and Medical Chemistry, University of Istanbul

Abstract

1. The specific precipitation of serum-pseudoglobulin by homologous antiserum is inhibited by introduction of approximately 100 or more azogroups per molecule of globulin (mol wt = 175,000) as well as by introduction of the same number of iodine atoms or N-acetyl groups. Azoglobulin, iodoglobulin, and acetylglobulin with less than about 50 substituting groups per molecule are precipitated exactly as well as native pseudoglobulin.

2. The precipitation of atoxylazoglobulin by an antiserum to atoxylazoglobulin is not inhibited by N-acetylation.

3. Our experiments indicate that the specificity of natural pseudoglobulin is not determined by a single "determinant group", but by a definite "determinant arrangement" of tyrosine groups, free amino groups and perhaps further groups on the surface of the proteic molecule. Such determinant arrangements seem to be responsible for the specificity of native proteins.