Etude de la L(+) - lactate: cytochrome c oxydoréductase (cytochrome b2) de la levure Hansenula anomala

摘要: Summary We describe first a simple method for preparing pure L(+) lactate: cytochrome c oxidoreductase (EC 1.1.2.3) or b2 from the yeast Hansenula anomala. The purification procedure includes autolysis of freeze-dried followed by fractionations with chilled acetone then ammonium sulfate; chromatography on DEAE-cellulose is eventually employed. non-crystalline enzyme samples can be conveniently preserved long periods as precipitate in sulfate but minor inactivation. In second part this paper presented comparison some physical-chemical and enzymatic properties new that crystalline purified Saccharomyces cerevisiae. Both enzymes are tetrameric flavo-hemoproteins nearly identical molecular weight shape catalyze specifically oxidation isomer lactate presence dyes ferricytochrome c. Considering its very high activity capability to inhibited an excess substrate, anomala resembles more closely «physiological form ( Somlo , M. Slonimski P., Bull. Soc. Chimie Biol., 48 (1966) 1221) than