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

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

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.

Full Text

Restricted Access

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

References

  1. Li T., Yuan D., Yuan J. // Adv. Exp. Med. Biol. 2020. V. 1177. P. 101–131.
  2. Barzkar N., Jahromi S. T., Vianello F. // Mar. Drugs. 2022. V. 20. № 1. P. 46. https://doi.org/10.3390/md20010046
  3. Zhang S., Wang Y., Zhang N., Sun Z., Shi Y., Cao X., Wang H. // Food Technol. Biotechnol. 2015. V. 53. № 2. P. 243–248.
  4. Duan Y., Katrolia P., Zhong A., Kopparapu N. K. // Prep. Biochem. Biotechnol. 2022. V. 52. № 9. P. 1008–1018.
  5. Zhao L., Lin X., Fu J., Zhamg J., Tang W., He Z. // Mar. Drugs. 2022. V. 20. № 6. P. 356. https://doi.org/10.3390/md20060356
  6. Батомункуева Б. П., Егоров Н. С. // Микробиология. 2001. Т. 70. № 5. С. 602–606.
  7. Осмоловский А. А., Звонарева Е. С., Крейер В. Г., Баранова Н. А., Егоров Н. С. // Биоорганическая химия. 2014. Т. 40. № 6. С. 688–694.
  8. Звонарева Е. С., Осмоловский А. А., Крейер В. Г., Баранова Н. А., Котова И. Б., Егоров Н. С. // Биоорганическая химия. 2015. Т. 41. № 5. С. 559–564.
  9. Laemly U. K. // Nature. 1970. V. 227. № 5259. P. 680–685.
  10. Hu Y., Yu D., Wang Z., Hou J., Tyagi R., Liang Y., Hu Y. // Scientific Reports. 2019. V. 9. № 9235. https://doi.org/10.1038/s41598-019-45686-y
  11. Thornton D. J., Carlstedt I., Sheehan J. K. // Methods Mol. Biol. 1994. V. 32. P. 119–128.
  12. Звонарева Е. С., Осмоловский А. А., Крейер В. Г., Баранова Н. А., Котова И. Б., Егоров Н. С. // Прикл. биохимия и микробиология. 2018. Т. 54. № 2. С. 195–200.
  13. Proteolytic Enzymes. A practical approach. / Ed. R. Beynon, J. S. Bond. Oxford: Oxford Univ. Press, 2001. 340 p.
  14. Biaggio R. T., Silva R. R., Rosa N. G., Leite R. S., Arantes E. C., Cabral T. P., Juliano M. A., Juliano L., Cabral H. // Prep. Biochem. Biotechnol. 2016. V. 46. № 3. P. 298–304.
  15. Осмоловский А. А., Крейер В. Г., Баранова Н. А., Кураков А. В., Егоров Н. С. // Прикл. биохимия микробиология. 2015. Т. 51. № 1. С. 86–92.
  16. Das A. K., Bellizzi J. J., Tandel S., Biehl E., Clardy J., Hofmann S. L. // J. Biol. Chem. 2000. V. 275. № 31. P. 23847–23851.
  17. Richmond G. S., Smith T. K. // Biochem. J. 2007. V. 405. № 2. P. 319–329.
  18. Chakrabarti S. K., Matsumura N., Ranu R. S. // Curr. Microbiol. 2000. V. 40. № 4. P. 239–244.
  19. Звонарева Е. С., Осмоловский А. А., Баранова Н. А., Котова И. Б., Крейер В. Г. // Прикл. биохимия и микробиология. 2023. Т. 59. № 4. С. 369–375.

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
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).

Download (88KB)
Indexing metadata
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.

Download (75KB)
Indexing metadata
4. Fig. 3. Effect of pH (a) and temperature (b) on the activity (1) and stability (2) of protease of A. tabacinus BEOFB3260m.

Download (114KB)
Indexing metadata

Copyright (c) 2024 Russian Academy of Sciences