A new subunit of horse liver alcohol dehydrogenase and subunit composition of the polymorphic form.
The most cathodal (on starch-gel electrophoresis), steroid-active band of horse liver alcohol dehydrogenase, whose catalytic properties were shown to be dependent on the livers used as a starting material [Pietruszko (1974) Biochem. Biophys. Res. Commun. 60, 687-694], has been prepared from A-type and S-type horse livers by identical methods. Results presented here show that different isoenzymes are present in these preparations.
D000429:Alcohol Oxidoreductases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D000577:Amides / Q000037:antagonists & inhibitors; D000818:Animals; D000440:Butanols / Q000494:pharmacology; D004592:Electrophoresis, Starch Gel; D006736:Horses; D006358:Hot Temperature; D006914:Hydroxysteroids / Q000378:metabolism; D007527:Isoenzymes / Q000032:analysis*; D007700:Kinetics; D008095:Lithocholic Acid / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D013256:Steroids / Q000378:metabolism
D000577:Amides; D000440:Butanols; D006914:Hydroxysteroids; D007527:Isoenzymes; D013256:Steroids; D008095:Lithocholic Acid; D000429:Alcohol Oxidoreductases