Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme
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چکیده
منابع مشابه
Histological distribution of class III alcohol dehydrogenase in human brain.
The distributions of class III alcohol dehydrogenase (ADH), a glutathione-dependent formaldehyde dehydrogenase, and class I ADH in the human brain were examined immunohistochemically. The most intense immunostaining of class III ADH was observed in the dendrites and cytoplasm of cerebellar Purkinje cells. Scattered cerebral cortical neurons in layers IV and V, and some hippocampal pyramidal neu...
متن کاملA New View of Alcohol Metabolism and Alcoholism—Role of the High-Km Class III Alcohol Dehydrogenase (ADH3)
The conventional view is that alcohol metabolism is carried out by ADH1 (Class I) in the liver. However, it has been suggested that another pathway plays an important role in alcohol metabolism, especially when the level of blood ethanol is high or when drinking is chronic. Over the past three decades, vigorous attempts to identify the enzyme responsible for the non-ADH1 pathway have focused on...
متن کاملS-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme.
An enzyme isolated from rat liver cytosol (native molecular mass 78. 3 kDa; polypeptide molecular mass 42.5 kDa) is capable of catalysing the NADH/NADPH-dependent degradation of S-nitrosoglutathione (GSNO). The activity utilizes 1 mol of coenzyme per mol of GSNO processed. The isolated enzyme has, as well, several characteristics that are unique to alcohol dehydrogenase (ADH) class III isoenzym...
متن کامل[Allosterism of acidic alcohol dehydrogenase (class III ADH) of mouse liver and its role in alcohol metabolism].
Two major ADH isozymes of mouse liver, basic ADH (Class I) and acidic ADH (Class III) were purified and the effects of various hydrophobic substances (t-butanol, butyramide, trifluoroethanol, trichloroacetic acid, stearic acid, oleamide, phenylalanine and norleucine) on their activities were investigated. All these hydrophobic substances activated acidic ADH with a range of from 15 to 560%, and...
متن کاملAlcohol 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 ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2004
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(03)01524-2