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.
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology|
|Publication status||Published - Dec 1992|
ASJC Scopus subject areas
- Molecular Biology