Regulation of methemoglobin reduction in human erythrocytes.
نویسندگان
چکیده
منابع مشابه
[Regulation of methemoglobin reduction in human erythrocytes].
The regulation of methemoglobin reduction in human erythrocytes was studied in vitro in association with glycolytic reactions, by using hemolysates prepared from the nitrate-treated eryth rocytes. The results obtained are as follows; 1) The addition of cytochrome b5 to the reaction mixture containing fructose 1,6-diphosphate as the substrate for glycolysis caused a marked increase in...
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THE BASIS FOR EDTA-STIMULATION OF METHEMOGLOBIN REDUCTION IN HEMOLYSATES OF HUMAN ERYTHROCYTES Lucy Jean Sannes* and Donald E. Hultquist ** Department of Biological Chemistry The University of Michigan Ann Arbor, Michigan 48109 Received November lo,1979 Summary: We have studied the stimulation by EDTA of methemoglobin reduction in hemolysates of human erythrocytes. The EDTA effect has been show...
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We have examined the structure-activity relationships in methemoglobin (MetHb) formation by high explosives 2,4,6-trinitrotoluene (TNT), 2,4,6-trinitrophenyl-N-nitramine (tetryl) and 2,4,6-trinitrophenyl-N-nitraminoethylnitrate (pentryl), and a number of model nitrobenzenes. In lysed human erythrocytes the rate constants of oxyhemoglobin (OxyHb) oxidation increased with an increase in single-el...
متن کاملPurification of reduced pyridine nucleotide dehydrogenase from human erythrocytes and methemoglobin reduction by the enzyme.
Reduced pyridine nucleotide dehydrogenase was purified 44,000-fold from normal human erythrocytes by procedures including ammonium sulfate fractionation, calcium phosphate gel chromatography, Sephadex G-100 gel filtration, and isoelectric focusing. The most purified enzyme preparation showed a single homogeneous peak (s~~,~ = 2.77 S) upon ultracentrifugation and was nearly homogeneous on acryla...
متن کاملProperties of methemoglobin reductase and kinetic study of methemoglobin reduction.
A soluble erythrocyte cytochrome b5 was purified as the substrate of methemoglobin reductase and an electron carrier to methemoglobin. The isoelectric point of this protein was at pH 4.3, and E0' was -0.010 at pH 7.0.. The Km value of the enzyme for this protein was 1 x 10(-4) M, and the turnover number (k5) was 3.4 x 10(4) min-1, with NADH as an electron donor at pH 7.0. The optimum pH of the ...
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ژورنال
عنوان ژورنال: Journal of Nippon Medical School
سال: 1987
ISSN: 0048-0444,1884-0108
DOI: 10.1272/jnms1923.54.590