Interactions between heparinoids and alcohol dehydrogenase

Redox interactions between catalase and alcohol dehydrogenase pathways of ethanol metabolism in the perfused rat liver.

Alcohol metabolism via alcohol dehydrogenase (ADH) and catalase was studied in perfused rat livers by measuring the oxidation of methanol and butanol, selective substrates for catalase and ADH, respectively. In livers from fasted rats, basal rates of methanol uptake of 15 +/- 1 mumol/g/h were decreased significantly to 8 +/- 2 mumol/g/h by addition of butanol. Concomitantly, pyridine nucleotide...

ALCOHOL DEHYDROGENASE: Structure and Function

Drosophila Alcohol Dehydrogenase

Drosophila alcohol dehydrogenasc (alcohol:NADf oxidorcduct.ase, EC 1.1.1.1) has attracted attention in several laboratories (l-3) recently. Genetic variants of this enzyme were found, and consequently it was possible to determine its structural locus on the genetic map. The specific activity of alcohol dehydrogenase varies greatly along the t.ime axis of devcloprnent of this organism, and it oc...

Alcohol dehydrogenase isoenzymes nomenclature.

We read with a great pleasure the article ‘Rare ADH variant constellations are specific for alcohol dependence’ by Zuo et al. (2012). We want to direct the speciality about the alcohol dehydrogenase (ADH) isoenzyme nomenclature to the readers of Alcohol and Alcoholism. Namely, the authors use an old isoenzyme nomenclature what can cause some confusion to not enough familiar readers. Electrophor...

Alcohol Dehydrogenase with

Complexation of alcohol dehydrogenase (ADH) and trypsin with poly(diallyldimethyl-ammonium chloride) (PDADMAC) in dilute electrolyte solution was studied by turbidimetric titration, quasi-elastic light scattering (QELS), and electrophoretic light scattering (ELS). Both QELS and turbidimetric titration show that PDADMAC forms complexes with ADH and trypsin in 0.01M NaCl solution at pH ¢ 6.8 and ...