HYDROLYSIS OF PROTEINS BY COLLAGENOLYTIC PROTEASES FROM KING CRAB

Hydrolysis of collagen molecules in the presence of collagenolytic pro teases A and C from the king crab has been studied by electrophoresis. Both proteases are shown to hydrolyze effectively type I and III coll agens, patterns of the products differing for the proteases A and C. T he thermal denaturation of the type I collagen increased the effective ness of the enzymatic hydrolysis. The crab collagenolytic proteases ca talyze the hydrolysis of such proteins as bovine serum albumin, ovalbu min, horse cytochrome c, mouse immunoglobulin G, casein and human fibr inogen, only elastin being resistant. The mechanisms of the fibrinogen cleavage differ not only for the proteases A and C but also for plasm in, whereas the efficiencies in all the cases are similar.