Reactions of 4-dimethylaminophenol with hemoglobin, and autoxidation of 4-dimethylaminophenol.

doi:10.1016/0009-2797(74)90076-3

Paper

Reactions of 4-dimethylaminophenol with hemoglobin, and autoxidation of 4-dimethylaminophenol.

Published 1974 · P. Eyer, M. Kiese, G. Lipowsky

Chemico-biological interactions

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45

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Abstract

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In Vitro Study

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4-dimethylaminophenol can catalyze ferrihemoglobin formation, oxidize 4-dimethylaminophenol, and produce various products, including hydroquinone, 4-methylaminophenol, 4-aminophenol, and a purple and yellow dye.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Reactions of 4-dimethylaminophenol with hemoglobin, and autoxidation of 4-dimethylaminophenol.

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References

Formation of ferrihaemoglobin with aminophenols in the human for the treatment of cyanide poisoning.

Aminophenols, such as 4-dimethylaminophenol and 4-methylaminophenol, rapidly produce ferrihaemoglobin in the blood, aiding in the treatment of cyanide poisoning without immediate cardiovascular system effects.

The differential reactivity of the oxidation products of o-aminophenols towards protein and nucleic acid.

Oxidation products of o-aminophenols combine with protein in vitro but not with nucleic acids, suggesting it is improbable that they react with nucleic acids in vivo.

The oxidation of o-aminophenols by cytochrome c and cytochrome oxidase. V. Inactivation of catalase and arginase by 2-imino-1,2-fluorenoquinone.

Oxidation of o-aminophenols by cytochrome c and cytochrome oxidase produces 2,3-fluorenoquinone, which interacts with bovine serum albumin in a model system.

The interaction of 2-amino-1-naphthol with bovine serum albumin and cytochrome c in relation to its effect on rat bladder.

2-amino-1-naphthol's interaction with rat bladder tissue leads to a 1,2-naphthoquinoneprotein derivative, which may play a role in bladder cancer susceptibility.

The oxidation of o-aminophenols by cytochrome c and cytochrome oxidase. I. Enzymatic oxidations and binding of oxidation products to bovine serum albumin.

Cytochrome c and cytochrome oxidase system may perform enzymatic oxidations of o-aminophenols, leading to quinonoid intermediates that bind readily to bovine serum albumin in vitro.

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