PROTEINASE BIOSYNTHESIS BY STREPTOCOCCUS LIQUEFACIENS: I. THE EFFECT OF CARBON AND NITROGEN SOURCES, pH, AND INHIBITORS

Abstract

Some nutritive aspects of proteinase biosynthesis by non-proliferating cells of Streptococcus liquefaciens, strain 31, were investigated by substituting constituents in a basal medium containing casein, lactose, purines, pyrimidines, vitamins, and salts. The casein of the medium could be replaced by a mixture of 12 "essential" amino acids (glutamic acid, histidine, valine, serine, methionine, leucine, isoleucine, arginine, cystine, lysine, tryptophane, and threonine), thus demonstrating that proteinase synthesis can occur in a medium devoid of protein. Proteinase biosynthesis appeared to depend upon an inordinately high concentration of arginine, required a fermentable carbohydrate, and occurred optimally at pH 6.3. Sodium fluoride and iodoacetate did not inhibit the proteinase activity but radically curbed its synthesis.