Collagenolytic activity of crustacean midgut serine proteases: comparison with the bacterial and mammalian enzymes.
1. We have investigated the collagenolytic activity of the following serine proteases: proteinase K, subtilisin Novo, Staphylococcal endoproteinase Glu-C, Streptomyces pronases, the trypsins and chymotrypsins from shrimp midgut and bovine pancreas. 2. By assays on both the insoluble 3H-collagen fibrils and the soluble type I collagen, it was demonstrated that the shrimp midgut serine proteases, and less efficiently, the pronases from Streptomyces griseus, could hydrolyze collagen while the other serine proteases tested could not. 3. Our data indicate that the trypsins and chymotrypsins of shrimp (Penaeus monodon) directly and indirectly digest native collagen, and that the indirect pathway probably involves activation of procollagenase in the native collagen by these serine proteases.
Chen
Y L
YL
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, Republic of China.
Lu
P J
PJ
Tsai
I H
IH
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D033364:Decapoda / Q000201:enzymology*; D004064:Digestive System / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D009842:Oligopeptides; C043307:succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide; D003094:Collagen; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin