Some Properties of Alkaline Protease in Rat Muscle Compared with That in Peritoneal Cavity Cells

Further studies were made on muscle alkaline protease and, at the same time, its properties were compared with those of the protease in peritoneal cavity cells. Both enzymes showed similar properties. Their molecular weight was 22,000, optimum temperature 57°C, optimum pH 9.0~10.5. They were slightly inhibited by soybean trypsin inhibitor. Tosylphenylalaninechloromethylketone inhibited both enzymes but tosyllysinechloromethylketone did not. Both enzymes cleaved peptide bonds Tyr (16)-Leu(17), Phe(24)-Phe(25) of oxidized B chain of insulin.