Результаты исследований: Научные публикации в периодических изданиях › статья
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.
в: Free Radical Research, Том 49, № 6, 2015, стр. 777-789.Результаты исследований: Научные публикации в периодических изданиях › статья
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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