Autor: |
Osmolovskiy, A., Sharkova, T., Matveeva, E., Kreier, V., Kurakov, A., Baranova, N., Egorov, N. |
Předmět: |
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Zdroj: |
Applied Biochemistry & Microbiology; Jan2016, Vol. 52 Issue 1, p31-35, 5p |
Abstrakt: |
The cultivation conditions (cultivation duration, nitrogen sources, and initial pH of the medium) of the strain Tolypocladium inflatum k1, a producer of extracellular proteases, has been optimized to achieve maximal plasminogen activator activity. It has been shown that Tolypocladium inflatum k1 forms at least two proteinases with activator activity towards plasminogen. One of them is thiol-dependent, EDTA-sensitive serine proteinase, which activates plasminogen and does not hydrolyze fibrin, indicating its higher specificity and prospects for the development of new thrombolytic agents. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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