| Abstract: | Six proteolytic fractions of the soyabean differed in specificity on synthetic substrates. Their Michaelis constants on poly (L-glutamic acid) differed one from the other. The optimum pH values of proteolytic action were slightly lower than that of the crude extract. The fractions did not autolyse, nor did one fraction hydrolyse any other. Finally, none of the fractions exhibited trypsin-like activity, as characterised by ability to hydrolyse benzoylarginine ethyl ester, either at their optimum pH or at the pH optimum of trypsin. |
