Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
TLDR
Glutathione peroxidase activity is found to be associated with a relatively stable, nondialyzable, heat-labile, intracellular component which is separable from hemoglobin, by gel filtration and ammonium sulfate precipitation.About:
This article is published in Journal of Laboratory and Clinical Medicine.The article was published on 1967-07-01 and is currently open access. It has received 10439 citations till now. The article focuses on the topics: Glutathione peroxidase & GPX5.read more
Citations
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Journal ArticleDOI
Glutathione peroxidase activity in selenium-deficient rat liver☆
TL;DR: Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration chromatogram of rat liver supernatant when 1.5 mM cumene hydroperoxide was used as substrate, and the second peak represents a second glutathienase activity which catalyzes the destruction of organic hydroperoxides but has little activity toward H 2 O 2 and which persists in severe selenium deficiency.
Book ChapterDOI
[44] Glutathione peroxidase
TL;DR: This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation.
Journal ArticleDOI
Review on in vivo and in vitro methods evaluation of antioxidant activity.
TL;DR: DPPH method was found to be used mostly for the in vitro antioxidant activity evaluation purpose while LPO was found as mostly used in vivo antioxidant assay.
Journal ArticleDOI
Measurement of superoxide dismutase, catalase, and glutathione peroxidase in cultured cells and tissue
TL;DR: General protocols are described to measure the antioxidant enzyme activity of superoxide dismutase (SOD), catalase and glutathione peroxidase, to evaluate the levels of the various antioxidant enzymes in tissues and cells.
Journal ArticleDOI
Lipid peroxidation in maternal and cord blood and protective mechanism against activated-oxygen toxicity in the blood
TL;DR: Sudden exposure of the newborn infant to a normobaric atmosphere after beginning breathing seems to cause oxidation of red blood cell membrane, denaturation of the membrane, inducing hemoglobin breakdown, and consequently hemolysis.
References
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Journal ArticleDOI
The Determination of Enzyme Dissociation Constants
Hans Lineweaver,Dean Burk +1 more
TL;DR: On the basis of the assumed theory the rate of the observed reaction is directly proportional to the concentration of the enzyme-substrate compound, where (E:l = (ES).
Journal Article
Improved method for the determination of blood glutathione.
Ernest Beutler,O Duron,B M Kelly +2 more
Journal ArticleDOI
The extinction coefficients of the reduced band of pyridine nucleotides
B.L. Horecker,Arthur Kornberg +1 more
TL;DR: The quantitative determination of the pyridine nucleotides and of substrates which can be brought into stoichiometric reaction with them has been hampered by the lack of reliable extinction coefficients for these substances.
Journal ArticleDOI
Enzymatic Deficiency in Primaquine-Sensitive Erythrocytes
Journal ArticleDOI
Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.
TL;DR: The most plausible route for the conversion of hemoglobin into biliverdin in vivo is through the oxidation and opening of the tetrapyrrole ring, after which the globin and iron are removed as discussed by the authors.