ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS

Abstract
E. coli tryptophan synthetase, the enzyme catalyzing the terminal step in fhe biosynthesis of tryptophan, was found to consist of 2 separable protein components, A and B. The properties of the purified components are given. Experiments were conducted on the reaction between proteins A and B and with small molecular weight intermediates of both compounds. Combination of the 2 components is responsible for the enzymatic action of tryptophan synthetase but available data do not permit any definite conclusions on the specific function of either moiety.

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