Abstract
1. An elastase-like enzyme was purified from the pyloric caeca of rainbow trout by hydrophobic interaction, cation exchange and gel-filtration chromatography. 2. The approximate molecular weight of the elastase was 27 kDa and the isoelectric point was remarkably basic. 3. The pH optimum of this enzyme was 8.0, when assayed with Succinyl-Ala-Ala-Ala-p-Nitroanilide. 4. When assayed with Succinyl-Ala-Ala-Ala-p-Nitroanilide, the enzyme activity had a temperature optimum of 45 degree C, and the enzyme was stable up to this temperature. 5. The trout elastase exhibited a higher specific activity than porcine elastase against Succinyl-Ala-Ala-Ala-p-Nitroanilide and elastin-orcein. 6. The trout elastase was inhibited by elastatinal, PMSF, TPCK, SBTI and Bowman-Birk inhibitor.
| Original language | English |
|---|---|
| Journal | Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology |
| Volume | 106 |
| Issue number | 2 |
| Pages (from-to) | 331-336 |
| Number of pages | 6 |
| ISSN | 1096-4959 |
| DOIs | |
| Publication status | Published - 1993 |
Keywords
- EC 2.5.1.18
- MUTATIONAL ANALYSIS
- TYROSINE-9
- Artiodactyla Mammalia Vertebrata Chordata Animalia (Animals, Artiodactyls, Chordates, Mammals, Nonhuman Vertebrates, Nonhuman Mammals, Vertebrates) - Suidae [85740] Suidae
- Pisces Vertebrata Chordata Animalia (Animals, Chordates, Fish, Nonhuman Vertebrates, Vertebrates) - Osteichthyes [85206] Osteichthyes
- ELASTASE 9004-06-2
- 10010, Comparative biochemistry
- 10060, Biochemistry studies - General
- 10064, Biochemistry studies - Proteins, peptides and amino acids
- 10506, Biophysics - Molecular properties and macromolecules
- 10614, External effects - Temperature as a primary variable
- 10802, Enzymes - General and comparative studies: coenzymes
- 10806, Enzymes - Chemical and physical
- 14004, Digestive system - Physiology and biochemistry
- Biochemistry and Molecular Biophysics
- Ingestion and Assimilation
- Digestive System
- Enzymology