Doxorubicin inhibits oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) by a lactoperoxidase/H2O2 system by reacting with ABTS-derived radical
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چکیده
منابع مشابه
Colorimetry of hemoglobin in plasma with 2,2'-azino-di(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS).
Hemoglobin in plasma can be determined by the color-developing action of 2,2'-azino-di(3-ethylbenzthiazoline-6-sulfonic acid), which is oxidized to a colored form by a peroxidase-like effect of hemoglobin in the presence of hydrogen peroxide. Sensitivity, precision, and accuracy are discussed. The calibration curve is linear for hemoglobin concentrations up to 1 g/L; the minimum detectable conc...
متن کاملGender differences in antioxidant capacity of rat tissues determined by 2,2'-azinobis (3-ethylbenzothiazoline 6-sulfonate; ABTS) and ferric reducing antioxidant power (FRAP) assays.
Differences in susceptibility to oxidative stress between males and females have been postulated. Several methods have been developed to assess the total antioxidant capacity of human serum or plasma, but just recently some of them were employed for measurement of antioxidant capacity of tissues. In this study, we measured and compared antioxidant capacity of heart, kidney, liver and brain tiss...
متن کاملEvaluation of the spectrophotometric assay of guanase with 2,2'-azino-di(3-ethylbenzthiazoline-6-sulphonate) (ABTS) as chromogen.
A simple spectrophotometric assay for serum guanase based on the oxidation of 2,2'-azino-di(3-ethylbenzthiazoline-6-sulphate) (ABTS) using xanthine oxidase, uricase and peroxidase is described and statistically examined through its application to normal and pathological sera. The method is very sensitive, precise (CV below 8.13%) and linear up to 152.5 U/l. Comparison with the methods of Hue & ...
متن کاملInfluence of macromolecular crowding on the oxidation of ABTS by hydrogen peroxide catalyzed by HRP
متن کامل
Oxidation of ABTS by silicate-immobilized cytochrome c in nonaqueous solutions.
Cytochrome c can be readily adsorbed onto mesoporous silicates at high loadings of up to 10 mmol g(-)(1) of silicate. The adsorbed protein retains its peroxidative activity, with no diffusional limitations being observed. The protein can be adsorbed onto the external surface of the silicate or, provided that the pore diameter is sufficiently large, into the channels. In aqueous buffer, the cata...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2007
ISSN: 0003-9861
DOI: 10.1016/j.abb.2007.06.027