Purification and characterization of a trypsin-like enzyme from the hepatopancreas of crayfish (Procambarus clarkii)

N. Guizani, M. R. Marshall, C. I. Wei

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1. 1. A trypsin-like enzyme was purified from the hepatopancreas of Louisiana swamp crayfish, Procambarus clarkii, by a combination of hydrophobic interaction chromatography, molecular sieving and ion-exchange chromatography. 2. 2. The enzyme had a molecular weight of 33.6 kDa on SDS-PAGE and an isoelectric point of 3.0. 3. 3. The enzyme exhibited optimal activity at pH 8.0 and an optimal temperature of 55°C. It was stable in the pH range of 7.5-9.0, but unstable above 55°C. 4. 4. The tryptic activity was inhibited by phenylmethyl sulfonyl fluoride and other well-established trypsin inhibitors. 5. 5. Immunological study showed that crayfish trypsin-like enzyme shared structural components with bovine trypsin.

Original languageEnglish
Pages (from-to)809-815
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number4
Publication statusPublished - 1992


ASJC Scopus subject areas

  • Biochemistry
  • Physiology

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