AN IMMUNOLOGICAL STUDY OF MUTANTS OF ESCHERICHIA COLI LACKING THE ENZYME TRYPTOPHAN SYNTHETASE

Abstract

The characteristics of the neutralization of E. coll tryptophan synthetase by rabbit antibody are described. Using this system extracts from 3 groups of mutants lacking tryptophan synthetase were examined for cross-reacting materials capable of removing antibody to the enzyme. One group of mutants formed a protein which was immunologically similar to tryptophan synthetase. The other 2 groups did not form any cross-reacting materials. These latter groups differed from the first group in that they also lacked an enzyme involved in the conversion of indole glycerol phosphate to indole. On the basis of this correlation it was suggested that the cross-reacting protein may be an enzyme involved in indole synthesis.