Isolation and characteristics of α-fibrinogenase venom from Naja oxiana
| Autor: | E. S. Yunusova, E. S. Sadykov, N. M. Sultanalieva, A. V. Shkinev |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
chemistry.chemical_classification
Metalloproteinase Chromatography biology Naja Ion chromatography Venom Plant Science General Chemistry Fibrinogen biology.organism_classification Molecular biology General Biochemistry Genetics and Molecular Biology Enzyme chemistry medicine Zymography Thermolabile medicine.drug |
| Zdroj: | Chemistry of Natural Compounds. 49:712-715 |
| ISSN: | 1573-8388 0009-3130 |
| DOI: | 10.1007/s10600-013-0714-x |
| Popis: | Venom of the Central Asian cobra (Naja oxiana Eichwald, NO) was shown to contain proteinase activity that cleaved the fibrinogen α-chain. An electrophoretically homogeneous preparation of basic (pI ~ 10) α-fibrinogenase (α-Fg) with MW 60 kDa exhibited the maximum activity at pH 6.0–8.0. α-Fg was a metalloproteinase (activity suppressed only by EDTA) that was thermolabile; at optimum temperature of 20–40°C (heating for 15 min at 60°C led to an activity loss of 80–85%). The enzyme cleaved dose-dependently the Aα-chain. The α-chain of human fibrinogen was hydrolyzed completely in 20 min with an experimental dose of 15 μg. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|