Abstract
Nine proteases, the main components of the collagenolytic complex from hepatopancreas ofParalithodes camtschatica crab have been isolated by gel filtration and FPLC, including ion-exchange chromatography on DEAE-Toyo-Pearl 650M and Mono-Q columns and hydrophobic interaction chromatography on a Phenyl-Superose column. Molecular weights of the resultant proteases were 36, 35 (2 proteins), 32, 28, 25 (3 proteins), and 23 kD (according to SDS-PAAG electrophoresis and HPLC on a Zorbax GF-250 column). N-terminal analysis showed that six proteases were trypsin-like enzymes homologous to digestive trypsins from other sources. One protease (23 kD) was related toAstacus fluviatilis metalloprotease and two others (32 and 35 (I) kD possess unique N-terminal sequences.
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