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Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. / Sokolov, A.V.; Kostevich, V.A.; Kozlov, S.O.; Donskyi, I.S.; Vlasova, I.I.; Rudenko, A.O.; Zakharova, E.T.; Vasilyev, V.B.; Panasenko, O.M.

In: Free Radical Research, Vol. 49, No. 6, 2015, p. 777-789.

Research output: Contribution to journalArticle

Harvard

Sokolov, AV, Kostevich, VA, Kozlov, SO, Donskyi, IS, Vlasova, II, Rudenko, AO, Zakharova, ET, Vasilyev, VB & Panasenko, OM 2015, 'Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines', Free Radical Research, vol. 49, no. 6, pp. 777-789. https://doi.org/10.3109/10715762.2015.1017478

APA

Sokolov, A. V., Kostevich, V. A., Kozlov, S. O., Donskyi, I. S., Vlasova, I. I., Rudenko, A. O., Zakharova, E. T., Vasilyev, V. B., & Panasenko, O. M. (2015). Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. Free Radical Research, 49(6), 777-789. https://doi.org/10.3109/10715762.2015.1017478

Vancouver

Author

Sokolov, A.V. ; Kostevich, V.A. ; Kozlov, S.O. ; Donskyi, I.S. ; Vlasova, I.I. ; Rudenko, A.O. ; Zakharova, E.T. ; Vasilyev, V.B. ; Panasenko, O.M. / Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. In: Free Radical Research. 2015 ; Vol. 49, No. 6. pp. 777-789.

BibTeX

@article{b72e8ed290ae43959da55b3feff227af,
title = "Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines",
abstract = "Myeloperoxidase (MPO) is a challenging molecular target which, if put under control, may allow regulating the development of inflammatory reactions associated with oxidative/halogenative stress. In this paper, a new kinetic method for assaying the halogenating activity of MPO is described. The method is based on measuring the rate of iodide-catalyzed oxidation of celestine blue B (CB) by oxygen and taurine N-chloramine (bromamine). The latter is produced in a reaction of taurine with HOCl (HOBr). CB is not a substrate for the peroxidase activity of MPO and does not react with hydrogen peroxide and superoxide anion radical. Taurine N-chloramine (bromamine) reacts with CB in molar ratio of 1:2. Using the new method, we studied the dependence of MPO activity on concentration of substrates and inhibitors. The specificity of MPO inhibition by non-proteolyzed ceruloplasmin is characterized. The inhibition of taurine N-chloramine production by neutrophils and HL-60 cells in the presence of MPO-affecting substances i",
keywords = "HOCl, celestine blue B, ceruloplasmin, halogenating activity, myeloperoxidase, taurine",
author = "A.V. Sokolov and V.A. Kostevich and S.O. Kozlov and I.S. Donskyi and I.I. Vlasova and A.O. Rudenko and E.T. Zakharova and V.B. Vasilyev and O.M. Panasenko",
year = "2015",
doi = "10.3109/10715762.2015.1017478",
language = "English",
volume = "49",
pages = "777--789",
journal = "Free Radical Research",
issn = "1071-5762",
publisher = "Informa Healthcare",
number = "6",

}

RIS

TY - JOUR

T1 - Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines

AU - Sokolov, A.V.

AU - Kostevich, V.A.

AU - Kozlov, S.O.

AU - Donskyi, I.S.

AU - Vlasova, I.I.

AU - Rudenko, A.O.

AU - Zakharova, E.T.

AU - Vasilyev, V.B.

AU - Panasenko, O.M.

PY - 2015

Y1 - 2015

N2 - Myeloperoxidase (MPO) is a challenging molecular target which, if put under control, may allow regulating the development of inflammatory reactions associated with oxidative/halogenative stress. In this paper, a new kinetic method for assaying the halogenating activity of MPO is described. The method is based on measuring the rate of iodide-catalyzed oxidation of celestine blue B (CB) by oxygen and taurine N-chloramine (bromamine). The latter is produced in a reaction of taurine with HOCl (HOBr). CB is not a substrate for the peroxidase activity of MPO and does not react with hydrogen peroxide and superoxide anion radical. Taurine N-chloramine (bromamine) reacts with CB in molar ratio of 1:2. Using the new method, we studied the dependence of MPO activity on concentration of substrates and inhibitors. The specificity of MPO inhibition by non-proteolyzed ceruloplasmin is characterized. The inhibition of taurine N-chloramine production by neutrophils and HL-60 cells in the presence of MPO-affecting substances i

AB - Myeloperoxidase (MPO) is a challenging molecular target which, if put under control, may allow regulating the development of inflammatory reactions associated with oxidative/halogenative stress. In this paper, a new kinetic method for assaying the halogenating activity of MPO is described. The method is based on measuring the rate of iodide-catalyzed oxidation of celestine blue B (CB) by oxygen and taurine N-chloramine (bromamine). The latter is produced in a reaction of taurine with HOCl (HOBr). CB is not a substrate for the peroxidase activity of MPO and does not react with hydrogen peroxide and superoxide anion radical. Taurine N-chloramine (bromamine) reacts with CB in molar ratio of 1:2. Using the new method, we studied the dependence of MPO activity on concentration of substrates and inhibitors. The specificity of MPO inhibition by non-proteolyzed ceruloplasmin is characterized. The inhibition of taurine N-chloramine production by neutrophils and HL-60 cells in the presence of MPO-affecting substances i

KW - HOCl

KW - celestine blue B

KW - ceruloplasmin

KW - halogenating activity

KW - myeloperoxidase

KW - taurine

U2 - 10.3109/10715762.2015.1017478

DO - 10.3109/10715762.2015.1017478

M3 - Article

VL - 49

SP - 777

EP - 789

JO - Free Radical Research

JF - Free Radical Research

SN - 1071-5762

IS - 6

ER -

ID: 3937833