Isolation and characterization of shrew (Suncus murinus) liver alcohol dehydrogenases.
1. Starch gel electrophoresis of adult shrew (Suncus murinus) liver extracts revealed five forms of alcohol dehydrogenase (ADH 1-5) and four of them were purified. 2. ADH-4 and ADH-5 resemble human class I ADH in terms of electrophoretic mobility, substrate specificity and sensitivity to pyrazole inhibition. 3. ADH-2 does not belong to any of the three classes of human ADHs but rather with catalytic properties similar to those of the class B ADH found in guinea pig liver. 4. ADH-1 prefers secondary alcohol over primary alcohol substrates and between the enantiomers tested, the enzyme favors the S isomers.
Keung
W M
WM
Department of Biochemistry, Chinese University of Hong Kong, Shatin, New Territories.
Ho
Y W
YW
Fong
W P
WP
Lee
C Y
CY
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D000077604:Fomepizole; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011720:Pyrazoles / Q000494:pharmacology; D012788:Shrews / Q000378:metabolism*; D013379:Substrate Specificity
D007527:Isoenzymes; D011720:Pyrazoles; D000077604:Fomepizole; D000429:Alcohol Oxidoreductases