Abstract
Low tryptophan synthase (L-serine hydro-lyase (adding indole), EC 4.2.1.20) activity in extracts of pea roots is a consequence of both a low concentration of the enzyme in roots and the presence of inhibitors at least some of which may be removed by homogenizing the fresh tissue with acetone. Inhibition by root extracts, and fractions thereof, was assayed against tryptophan synthase from seedling buds. At least three inhibitory components were detected, namely (1) a dialyzable, thermostabile component, (2) an undialyzable, thermolabile component, and (3) an undialyzable, thermostabile component. A dialyzable factor which protects an undialyzable inhibitory factor against heat inactivation is also indicated.Fractionation of crude root extracts by gel filtration on a column of Sephadex G-50 shows inhibitor with a molecular weight of about 10 000 or larger.
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