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Different Specificities in Antisera Prepared against Escherichia Coli Tryptophan Synthetase Subunit¹

From the Department of Biology, University of California, San Diego, P. O. Box 109, La Jolla, California 92037

Abstract

Four different antisera, prepared against purified Escherichia coli tryptophan synthetase subunit using different adjuvants and schedules of injection, were examined in detail.

Each antiserum demonstrated specificity for A gene product by not reacting detectably with extracts of certain mutants which had deletions or nonsense mutations in their A genes.

Two of the antisera appeared in every way to react only with active subunit enzyme. In contrast, the other two reacted at least partly with denatured molecules which could be produced by aging or by heating preparations containing subunit.

In micro-complement fixation assays the latter two sera showed a variety of reactions against extracts of strains with missense A gene mutations. These reactions could be misinterpreted as cross-reactions between the sera and native, homogeneous mutant subunit antigens.

The latter two sera also detected antigens in extracts of strains A109 and A229, strains in which A gene products had not before been demonstrated.

Footnotes

Supported in part by Atomic Energy Commission Contract AT (11-1)-34 and by Public Health Service Predoctoral Fellowship 1-F1-GM-33,440-02 (held by T.M.M.) from the National Institute of General Medical Sciences.

² Present address: Department of Biochemistry, University of Washington, Seattle, Washington 98105.