[Hydrolysis of proteins by collagenolytic proteinases from the king crab].
Hydrolysis of collagen molecules in the presence of collagenolytic proteases A and C from the king crab has been studied by electrophoresis. Both proteases are shown to hydrolyze effectively type I and III collagens, patterns of the products differing for the proteases A and C. The thermal denaturation of the type I collagen increased the effectiveness of the enzymatic hydrolysis. The crab collagenolytic proteases catalyze the hydrolysis of such proteins as bovine serum albumin, ovalbumin, horse cytochrome c, mouse immunoglobulin G, casein and human fibrinogen, only elastin being resistant. The mechanisms of the fibrinogen cleavage differ not only for the proteases A and C but also for plasmin, whereas the efficiencies in all the cases are similar.
Sakharov
I Iu
IIu
Litvin
F E
FE
Mit'kevich
O V
OV
D000818:Animals; D003386:Brachyura / Q000201:enzymology; D003094:Collagen / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D011489:Protein Denaturation; D011506:Proteins / Q000378:metabolism*
D011506:Proteins; D003094:Collagen; D010450:Endopeptidases
Gidroliz belkov kollagenoliticheskimi proteinazami kamchatskogo kraba.