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Collagenolytic protease complex fromParalithodes camtschatica hepatopancreas: Separation into individual components

  • Biophysics and Biochemistry
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Bulletin of Experimental Biology and Medicine Aims and scope

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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Correspondence to O. A. Klimova.

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Translated fromByulleten' Eksperimental'noi Biologii i Meditsiny, Vol. 128, No. 9, pp. 308–313, September, 1999

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Klimova, O.A., Chebotarev, V.Y. Collagenolytic protease complex fromParalithodes camtschatica hepatopancreas: Separation into individual components. Bull Exp Biol Med 128, 925–929 (1999). https://doi.org/10.1007/BF02438087

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  • DOI: https://doi.org/10.1007/BF02438087

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