Properties of Extracellular Protease — Regulator of Hemostasis Produced by Micromycete Aspergillus tabacinus

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Abstract

The extracellular protease with protein C-like and plasmin-like activities was isolated from the culture fluid of the micromycete A. tabacinus BEOFB3260m. It has been established that A. tabacinus extracellular protease is a non-glycosylated serine protease with mol. weight about 30 kDa. The enzyme is active and stable at temperature of 25–37°, active at pH 7.0–12.0 and stable at pH 3.0–12.0 and is a perspective candidate for new anticoagulant drugs development.

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About the authors

V. N. Lavrenova

Lomonosov Moscow State University

Author for correspondence.
Email: pkviktoria@mail.ru

Faculty of Biology

Russian Federation, Moscow, 119234

V. G. Kreyer

Lomonosov Moscow State University

Email: pkviktoria@mail.ru

Faculty of Biology

Russian Federation, Moscow, 119234

Z. Savkovic

University of Belgrade

Email: pkviktoria@mail.ru

Faculty of Biology

Serbia, Belgrade

A. A. Osmolovskiy

Lomonosov Moscow State University

Email: pkviktoria@mail.ru

Faculty of Biology

Russian Federation, Moscow, 119234

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Supplementary files

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2. Fig. 1. Isoelectric focusing of extracellular proteins of the culture fluid of A. tabacinus BEOFB3260m: 1 — pH, 2 — activity toward the substrate S-2366 (E × 10–3), 3 — A280, 4 — activity toward the substrate Chromozym TH (E × 10–3).

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3. Fig. 2. Electrophoretic analysis of extracellular protease of A. tabacinus in PAGE with SDS-Na: M — markers; 1 — electrophoretogram according to Laemmli; 2 — staining for the presence of a carbohydrate component; 3 — casein zymogram.

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4. Fig. 3. Effect of pH (a) and temperature (b) on the activity (1) and stability (2) of protease of A. tabacinus BEOFB3260m.

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