| Abstract: | The enzyme hydrolysing N-benzoyl-D,L-arginine-p-nitroanilide (BAPA). is isolated from vetch seedlings and 1600-fold purified by means of chromatography on DEAE-cellulose, hdroxyapatite and gel filtration through Sephadex G-100. The preparation is chromatographically homogenous, but disc electrophoresis in polyacrylamide gel revealed an insignificant contamination by inactive proteins. The data of disc electrophoresis in polyacrylamide gel in the presence of sodium dodecylsulphate have shown that BAPAase has a quaternary structure containing, probably, four subunits identical in their molecular weight. BAPAase has a narrow substrate specificity: it hydrolyses BAPA, benzoyl-D,L,-argininenaphtylamide, benzoyl-L-arginyglycine CBZ-L-arginylglycine histones and protamine, but does not attack L-arginyl-p-nitroanilide benzoyl-L-arginineamide, tosyl-L-arginine methyl ester and casein. |
