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Production of proteinase–plasminogen activators by micromycete Tolypocladium inflatum k1

Production of proteinase–plasminogen activators by micromycete Tolypocladium inflatum k1 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Production of proteinase–plasminogen activators by micromycete Tolypocladium inflatum k1

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References (1)

Publisher
Springer Journals
Copyright
Copyright © 2016 by Pleiades Publishing, Inc.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683816010129
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Nov 10, 2016

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