Isoenzymes of Drosophila Alcohol Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Interconversion of Isoenzymes of Drosophila Alcohol Dehydrogenase
Drosophila alcohol dehydrogenase and its subunits were examined for their physical characteristics. The intact enzyme was shown to have a molecular weight of approximately 60,000. The smallest apparent subunit was obtained by dissociating the enzyme with sodium dodecylsulfate and the molecular weight obtained was 7,500. Evidence for three partially dissociated forms was obtained; the subunits o...
متن کاملAlcohol 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...
متن کاملDrosophila 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...
متن کاملActivity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in sera of patients with hepatitis C
Introduction The changes of enzyme activity in the hepatocytes in the course of different liver diseases are reflected by increase of the corresponding enzyme activity in the plasma. For example, the activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) correlate with the severity of the condition during cirrhosis. In this study we measured the activity of ADH isoenzymes a...
متن کاملDrosophila melanogaster alcohol dehydrogenase: product-inhibition studies.
The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63291-0