Isoenzymes of alcohol dehydrogenase in retinoid metabolism.
作者： Xavier Parés , Pere Julià
DOI: 10.1016/0076-6879(90)89319-D
关键词: Retinol 、 Starch gel electrophoresis 、 Enzyme 、 Biochemistry 、 Metabolism 、 Alcohol dehydrogenase 、 Isozyme 、 Molecular biology 、 Biology 、 Substrate (chemistry) 、 Ethanol
摘要: Publisher Summary Alcohol dehydrogenase (ADH) is an enzyme widely distributed in animals, plants, and microorganisms. It catalyzes the reversible oxidation of a great variety alcohols to corresponding aldehydes ketones. ADH exhibits several isoenzymes most species studied. are very active toward long-chain hydrophobic alcohols. This chapter describes assay method ADH. heterogeneously animal tissues. Prior purification from particular organ it convenient analyze isoenzyme composition by starch gel electrophoresis. Procedures for mammalian have been reported. rat isoenzymes. Three detected tissues that named ADH-1, ADH-2, ADH-3 according their mobility on ADH-1 anodic form, characteristic stomach, ocular tissues, external epithelia. shows K m values 5 M ethanol 20 μM retinol has considered class II although no clear correspondence found with human
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