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- W114450991 abstract "Human whole blood and washed intact erythrocytes from human and sheep exhibit aniline hydroxylase activity indicative of oxygen activation by the erythrocytes. Formation of p-aminophenol by human and sheep erythrocytes was similar under similar conditions, 5.8 + 0.26 and 5.3 + 0.14 nmol ofp-aminophenol/ 60 min/ml, respectively, at 1 mM hemoglobin and 60 mM aniline. The amount of p-aminophenol produced was directly proportional to the concentration of oxyhemoglobin. Erythrocytes in which the hemoglobin had been oxidized completely to methemoglobin were essentially inert. Hence, oxyhemoglobin plays a key role in the catalysis. Furthermore, studies of the stimulatory effects of lactate, glucose, and methylene blue revealed that NADPH apparently is the important cofactor for the aniline hydroxylase activity of the erythrocytes. Thus, lactate which serves to produce NADH via the lactate dehydrogenase reaction had little, if any, effect on the hydroxylase activity, even under conditions where its ability to support reduction of methemoglobin was demonstrated. In contrast, the addition of glucose with methylene blue led to a 17-fold stimulation of the activity with both human and sheep erythrocytes. Glucose serves to supply the initial substrate for the pentose phosphate pathway which produces NADPH, and methylene blue predominantly affects NADPH-dependent electron transport. The combination of lactate with methylene blue produced no such stimulation." @default.
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- W114450991 date "1979-06-01" @default.
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- W114450991 title "Characterization of the aniline hydroxylase activity of erythrocytes." @default.
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- W114450991 doi "https://doi.org/10.1016/s0021-9258(18)50566-4" @default.
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