Five proteases designated as A ', A 2 , B, C and D were isolated from Euphausia superba by the succesive steps o f ammonium sulfate fractionation, acetone precipitation, gel filtration and DEAESephadex A-50 chromatography. A l , B, C and D were purified to homogeneity in disc gel electrophoresis by means of rechromatography on the DEAE-Sephadex A-50 column. Studies on substrate specificity of these enzymes revealed that A 2 , B, C and D were trypsin-like enzymes and A , a carboxypeptidase A . A ' , B, C and D had molecular weights of about 24,000, 24,000, 28,000 and 27,000; optimal pH a t 9.0, 8.0, 7.5 and 7.5-8.0; and optimal temperature at 48, 50, 55-60 and 55"C, respectively. The actiuity of B, C and D were not inhibited by sulfhydryl reagents and N-a-tosyl-L-phenylalanylchloro-methyl ketone, but inhibited by reducing agents, N-a-tosyl-L-lysylchloromethyl ketone and soybean trypsin inhibitor. The activity of protease A l was stimulated 3.5 fold by cobalt, but inhibited by 3-indolepropionate and D -p hen y la la n in e. vation of fresh krill and utilization of the enzymes. Noguchi et al.