Vanadium inhibition of serine and cysteine proteases
| Autor: | N. Guerrieri, Silvia Scippa, M. De Vincentiis, Paolo Cerletti, A. Salvati |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Proteases
Serine Proteinase Inhibitors Vanadium Compounds Physiology Proteolysis Cysteine Proteinase Inhibitors In Vitro Techniques Biochemistry Serine chemistry.chemical_compound Albumins Papain medicine Animals Trypsin Subtilisins Molecular Biology Serine protease medicine.diagnostic_test biology Subtilisin Caseins Vanadium Bromelains Cysteine protease Kinetics chemistry biology.protein Cattle Vanadates Oxidation-Reduction medicine.drug |
| Zdroj: | Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 122:331-336 |
| ISSN: | 1095-6433 |
| DOI: | 10.1016/s1095-6433(99)00014-8 |
| Popis: | A study was made on the effect of vanadium, in both the tetravalent state in vanadyl sulphate and in the pentavalent state in sodium meta-vanadate, and ortho-vanadate, on the proteolysis of azocasein by two serine proteases, trypsin and subtilisin and two cysteine proteases bromelain and papain. Also the proteolysis of bovine azoalbumin by serine proteases was considered. An inhibitory effect was present in all cases, except meta-vanadate with subtilisin. The oxidation level of vanadium by itself did not determine the inhibition kinetics, which also depended on the type and composition of the vanadium containing molecule and on the enzyme assayed. The pattern of inhibition was similar for proteases belonging to the same class. The highest inhibition was obtained with meta-vanadate on papain and with vanadyl sulphate on bromelain. |
| Databáze: | OpenAIRE |
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