Purification and characterization of a trypsin-like enzyme from the hepatopancreas of crayfish (Procambarus clarkii)
| Autor: | C.I. Wei, Maurice R. Marshall, Nejib Guizani |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Procambarus clarkii Chromatography Physiology Decapoda Hydrophilic interaction chromatography General Medicine Biology Trypsin biology.organism_classification Crayfish Biochemistry Enzyme Isoelectric point chemistry medicine Hepatopancreas Molecular Biology medicine.drug |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 103:809-815 |
| ISSN: | 0305-0491 |
| DOI: | 10.1016/0305-0491(92)90197-y |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|