抄録
Pro-proteinase C, the latent form of yeast proteinase C, was partially purified from the autolysate of baker's yeast. It was strongly activated by incubation at pH 5 or by treatment with urea or dioxane. The former activation was prevented by treatment to inactivate yeast proteinase A, which coexisted with the pro-enzyme in the present prepa-ration, but was promoted by addition of purified proteinase A. Thus, it was confirmed that A could activate pro-proteinase C. Furthermore, it was found that activation could be caused by extremes in pH or by heating to 55_??_60°C, accompanied by the simultane-ous destruction of the enzyme produced. Pro-proteinase C was stable over a range of pH 5 to 8 after 60 min incubation at 50°C.
