Differential susceptibility of human alcohol dehy drogenase isoenzymes to anions

FEBS Letters

Bühler, R.¹  Von Wartburg, J.-P.¹ 

[1] Medizinisch-chemisches Institut der Universität, Bühlstrasse 28, CH-3000 Bern 9, Switzerland

关键词: Alcohol dehydrogenase;    0Human liver isoenzyme;    Anion effect;   

DOI  :  10.1016/0014-5793(84)80610-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human liver alcohol dehydrogenase (ADH) isoenzymes β₁β₁, γ₁γ₁ from Caucasian individuals with ‘typical’ ADH and β₂β₂-Bern from Caucasian individuals with ‘atypical’ phenotype differed in their susceptibility to anions. At pH 7.0 β₁β₁ and γ₁γ₁ were more active in Tris-HCl buffer than in sodium phosphate buffer but less active in Hepes-NaOH and Mops-NaOH. β₂β₂-Bern showed the same activity in all these buffers. At pH 7.0 and at low concentrations (50–100 mM) chloride activated the ethanol oxidation by β₁β₁ and γ₁γ₁, whereas sulfate showed no effect. At anion concentrations above 100 mM all isoenzymes were inhibited. At pH 10.5 β₁β₁ and γ₁γ₁ were not activated. Measuring the acetaldehyde reduction, no comparable activation by chloride was observed; all three isoenzymes were inhibited, at significantly lower anion concentrations. These anion effects can be correlated with the different primary structures of the isoenzymes around the active site and the coenzyme binding site.

【 授权许可】

Unknown