Genetic Engineering Techniques: Recent Developments : Edited by P.C. Huang,T.T. Kuo and R. Wu Academic Press; New York, 1982 360 pages. $28.50

Extracts from white croaker skeletal muscle showed two alkaline proteases and a trypsin inhibitor when they were chromatographed in DEAE-Sephacel. The activity against azocasein was maximal at pH 8.5 and 9.1 for proteases I and II, respectively. Both enzymes showed optimum activity at 60° C. The molecular masses were found to be 132 kDa for protease 1,363 kDa for protease II, and 65 kDa for the inhibitor. Protease I showed the characteristics of a trypsin-like enzyme, and protease II those of a SH-enzyme. These proteins may play important roles in mechanisms of cellular proteolysis.