Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda).
1. Two chymotrypsin variants, with collagenolytic activities, were purified from the hepatopancreas of Penaeus vannamei using radioactive protein as the substrate. 2. These proteases are very close as far as amino acid composition, molecular weight, inhibitors studies and specificity against small synthetic substrates are concerned. 3. N-terminal amino acid sequences of both variants are identical and are very close to other known crustacean serine proteases.
Van Wormhoudt
A
A
Laboratoire de Biologie Marine, Collège de France, Concarneau.
Le Chevalier
P
P
Sellos
D
D
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin / Q000302:isolation & purification; D017364:Collagenases / Q000302:isolation & purification; D003445:Crustacea / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry; D033561:Penaeidae / Q000201:enzymology*; D010449:Peptide Mapping; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D013045:Species Specificity; D013379:Substrate Specificity
D000596:Amino Acids; D009842:Oligopeptides; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D017364:Collagenases