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- W142389323 abstract "This chapter focuses on the catalysis of methemoglobin reduction. It discusses the results of studies in which photometry and magnetic circular dichroism (MCD) spectroscopy were used to follow the kinetics of methemoglobin reduction. The chapter discusses an experimental study in which methemoglobin reduction in hemolysates was assayed. The hemolysate differs from conditions within the normal erythrocytes in that nitrite was added to convert hemoglobin to methemoglobin. The components of the cytoplasm were diluted by a factor of 4.8, the membranous fraction was removed, and NADH or NADPH was added to a concentration of 4 mM. In this system, the dependence of rate on the concentrations of the various components was studied by addition to the hemolysate of purified human methemoglobin, human erythrocyte cytochrome b5reductase, or bovine erythrocyte cytochrome b5. Direct reduction of methemoglobin by the addition of isolated ferrocytochrome b5was measured photometrically. The reaction was carried out at 37°C in a cuvette, which was already positioned in an Aminco recording spectrophotometer. Photochemical reduction mediated by lumiflavin 3-acetate was employed to reductively titrate mixtures of cytochrome b5and methemoglobin. MCD spectra were obtained with a Jasco J-40C spectropolarimeter equipped with an electromagnet. Spectra were acquired, stored, corrected, and analyzed by using a Nova III computer, a Tracor 1500N signal analyzer, an Ohio Scientific Challenger II microcomputer, and an ADM 3a terminal retrofitted with Retro-Graphics plotting hardware." @default.
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- W142389323 date "1984-01-01" @default.
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- W142389323 title "Catalysis of Methemoglobin Reduction" @default.
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- W142389323 doi "https://doi.org/10.1016/b978-0-12-152824-9.50033-2" @default.
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