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Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22. / Starikova, E.A.; Sokolov, A.V.; Vlasenko, A.Yu.; Burova, L.A.; Freidlin, I.S.; Vasilyev, V.B.

в: Biochemistry and Cell Biology, Том 94, № 2, 2016, стр. 129-137.

Результаты исследований: Научные публикации в периодических изданияхстатья

Harvard

Starikova, EA, Sokolov, AV, Vlasenko, AY, Burova, LA, Freidlin, IS & Vasilyev, VB 2016, 'Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22', Biochemistry and Cell Biology, Том. 94, № 2, стр. 129-137. https://doi.org/10.1139/bcb-2015-0069

APA

Starikova, E. A., Sokolov, A. V., Vlasenko, A. Y., Burova, L. A., Freidlin, I. S., & Vasilyev, V. B. (2016). Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22. Biochemistry and Cell Biology, 94(2), 129-137. https://doi.org/10.1139/bcb-2015-0069

Vancouver

Starikova EA, Sokolov AV, Vlasenko AY, Burova LA, Freidlin IS, Vasilyev VB. Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22. Biochemistry and Cell Biology. 2016;94(2):129-137. https://doi.org/10.1139/bcb-2015-0069

Author

Starikova, E.A. ; Sokolov, A.V. ; Vlasenko, A.Yu. ; Burova, L.A. ; Freidlin, I.S. ; Vasilyev, V.B. / Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22. в: Biochemistry and Cell Biology. 2016 ; Том 94, № 2. стр. 129-137.

BibTeX

@article{13c37b4b9f9c400d962328ea9a2214e2,
title = "Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22",
abstract = "Streptococcus pyogenes (group A Streptococcus – GAS) is an important gram-positive extracellular bacterial pathogen responsible for a number of suppurative infections. This microorganism developed complex virulence mechanisms to avoid host defense. We have previously revealed that Supernatant of Destroyed Streptococcal Cells (SDSC) from GAS type M22 causes endothelial cells{\textquoteright} dysfunction, inhibits cellular adhesion, migration, metabolism and proliferation in a dose-dependent manner without affecting cells{\textquoteright} viability. The present work is aimed at isolation and characterization of a component from GAS type M22 supernatant that suppresses proliferation of endothelial cells EA.hy926. Isolating a protein possessing antiproliferative activity allowed identifying arginine deiminase (AD). Further study showed that the enzyme is most active at pH 6.8. Calculating Km and Vmax gave the values of 0.67 mM and 42 s-1, respectively. Distinctive feature of AD purified from GAS type M22 is the closest to neutral pH optimum of",
keywords = "Streptococcus pyogenes M22, arginine deiminase, endothelial cell proliferation",
author = "E.A. Starikova and A.V. Sokolov and A.Yu. Vlasenko and L.A. Burova and I.S. Freidlin and V.B. Vasilyev",
year = "2016",
doi = "10.1139/bcb-2015-0069",
language = "English",
volume = "94",
pages = "129--137",
journal = "Biochemistry and Cell Biology",
issn = "0829-8211",
publisher = "National Research Council of Canada",
number = "2",

}

RIS

TY - JOUR

T1 - Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22

AU - Starikova, E.A.

AU - Sokolov, A.V.

AU - Vlasenko, A.Yu.

AU - Burova, L.A.

AU - Freidlin, I.S.

AU - Vasilyev, V.B.

PY - 2016

Y1 - 2016

N2 - Streptococcus pyogenes (group A Streptococcus – GAS) is an important gram-positive extracellular bacterial pathogen responsible for a number of suppurative infections. This microorganism developed complex virulence mechanisms to avoid host defense. We have previously revealed that Supernatant of Destroyed Streptococcal Cells (SDSC) from GAS type M22 causes endothelial cells’ dysfunction, inhibits cellular adhesion, migration, metabolism and proliferation in a dose-dependent manner without affecting cells’ viability. The present work is aimed at isolation and characterization of a component from GAS type M22 supernatant that suppresses proliferation of endothelial cells EA.hy926. Isolating a protein possessing antiproliferative activity allowed identifying arginine deiminase (AD). Further study showed that the enzyme is most active at pH 6.8. Calculating Km and Vmax gave the values of 0.67 mM and 42 s-1, respectively. Distinctive feature of AD purified from GAS type M22 is the closest to neutral pH optimum of

AB - Streptococcus pyogenes (group A Streptococcus – GAS) is an important gram-positive extracellular bacterial pathogen responsible for a number of suppurative infections. This microorganism developed complex virulence mechanisms to avoid host defense. We have previously revealed that Supernatant of Destroyed Streptococcal Cells (SDSC) from GAS type M22 causes endothelial cells’ dysfunction, inhibits cellular adhesion, migration, metabolism and proliferation in a dose-dependent manner without affecting cells’ viability. The present work is aimed at isolation and characterization of a component from GAS type M22 supernatant that suppresses proliferation of endothelial cells EA.hy926. Isolating a protein possessing antiproliferative activity allowed identifying arginine deiminase (AD). Further study showed that the enzyme is most active at pH 6.8. Calculating Km and Vmax gave the values of 0.67 mM and 42 s-1, respectively. Distinctive feature of AD purified from GAS type M22 is the closest to neutral pH optimum of

KW - Streptococcus pyogenes M22

KW - arginine deiminase

KW - endothelial cell proliferation

U2 - 10.1139/bcb-2015-0069

DO - 10.1139/bcb-2015-0069

M3 - Article

VL - 94

SP - 129

EP - 137

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 2

ER -

ID: 7564506