Determination of NADH2-ferricyanide oxidoreductase (cytochrome b5 reductase, diaphorase) activity of human erythrocytes by an analysis of the time-dependence of NADH2 oxidation

Papandreou, Photini; Rakitzis, Emmanuel T.

doi:10.1016/0009-8981(89)90187-3

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Clinica Chimica Acta

1989

DOI: 10.1016/0009-8981(89)90187-3

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Determination of NADH2-ferricyanide oxidoreductase (cytochrome b5 reductase, diaphorase) activity of human erythrocytes by an analysis of the time-dependence of NADH2 oxidation

Photini Papandreou

Emmanuel T. Rakitzis

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1992

2021

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Cited by 3 publications

References 7 publications

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A possible biological role of boar sperm diaphorase investigated by a specific monoclonal antibody

Mollova

Atanassov

Ivanova

et al. 1992

Animal Reproduction Science

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A possible biological role of boar sperm diaphorase investigated by a specific monoclonal antibody

Mollova

Atanassov

Ivanova

et al. 1992

Animal Reproduction Science

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Activity of membrane-bound NADH-methemoglobin reductase and physical state of lipids in erythrocyte membranes

Lukyanenko

Kozlova

Slobozhanina

2004

Bioelectrochemistry

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Lithium-induced modiphication of the physicochemical state of membrane proteins and lipids in human erythrocytes

Zubritskaya

Slobozhanina

2021

Vescì Akademìì navuk Belarusì. Seryâ biâlagičnyh navuk

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The effect of various concentrations of lithium sulfate on human erythrocytes in vitro has been studied. It has been shown that the effect of lithium salt in maximum pharmacological and toxic concentrations on cells leads to a modification of the physicochemical state of membrane-bound proteins and lipids. It was found that in human erythrocytes exposed to lithium ions, there is a decrease in the activity of membrane-bound acetylcholinesterase and methgemoglobin reductase, as well as a change in the microviscosity of the lipid bilayer of membranes. The results obtained can be used to create a cell test system for assessing the toxicity of lithium compounds.

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Determination of NADH2-ferricyanide oxidoreductase (cytochrome b5 reductase, diaphorase) activity of human erythrocytes by an analysis of the time-dependence of NADH2 oxidation

Cited by 3 publications

References 7 publications

A possible biological role of boar sperm diaphorase investigated by a specific monoclonal antibody

A possible biological role of boar sperm diaphorase investigated by a specific monoclonal antibody

Activity of membrane-bound NADH-methemoglobin reductase and physical state of lipids in erythrocyte membranes

Lithium-induced modiphication of the physicochemical state of membrane proteins and lipids in human erythrocytes

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