Drosophila alcohol dehydrogenase frequencies and temperature
نویسندگان
چکیده
منابع مشابه
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...
متن کاملDrosophila alcohol dehydrogenase. Purification and partial characterization.
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 کاملDrosophila Alcohol Dehydrogenase PURIFICATION AND PARTIAL
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 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 کاملInterconversion 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...
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ژورنال
عنوان ژورنال: Genetical Research
سال: 1978
ISSN: 0016-6723,1469-5073
DOI: 10.1017/s0016672300017845