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Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: pi-ADH.
- Source :
-
Biochemistry [Biochemistry] 1984 Dec 18; Vol. 23 (26), pp. 6363-8. - Publication Year :
- 1984
-
Abstract
- Homogeneous class II alcohol dehydrogenase (pi-ADH) has been isolated from human liver homogenates by chromatography on DE-52 cellulose, 4-[3-[N-(6-amino-caproyl)amino]propyl]pyrazole-Sepharose, SP-Sephadex C-50, and agarose-hexane-AMP, yielding an enzyme that has a significantly higher specific activity and is markedly more stable than that isolated by an earlier procedure. pi-ADH is composed of two identical 40 000-dalton subunits, contains 4 mol of zinc/dimer, and is readily inhibited by metal-chelating agents. The purified enzyme binds two molecules of coenzyme per dimer, exhibits an absorption maximum at 280 nm, epsilon 280 = 57 000, and exhibits an isoelectric point of 8.6. The class II isozyme catalyzes the oxidation of a variety of alcohols with Km values ranging from 7 microM to 560 mM and with kcat values from 32 min-1 to 600 min-1 and demonstrates a preference for hydrophobic substrates. The kcat/Km ratio for ethanol oxidation exhibits a pH maximum at 10.4.
- Subjects :
- Alcohol Dehydrogenase
Alcohol Oxidoreductases antagonists & inhibitors
Alcohol Oxidoreductases isolation & purification
Chelating Agents pharmacology
Humans
In Vitro Techniques
Isoenzymes antagonists & inhibitors
Isoenzymes isolation & purification
Kinetics
Substrate Specificity
Alcohol Oxidoreductases metabolism
Isoenzymes metabolism
Liver enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 23
- Issue :
- 26
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6397223
- Full Text :
- https://doi.org/10.1021/bi00321a012