[Ion-exchange chromatography on cholesterol oxidase from Actinomyces lavendulae on a Biocarb-type carboxyl cationite].
Reversible sorption on the Biocarb-D carboxyl cationite of cholesterol oxidase extracted from the mycelium of Actinomyces lavendulae was examined. Sorption at pH 5.0 and desorption at pH 5.5 maintained 80% of the enzyme activity and increased seven-fold the specific activity as calculated per protein. By gel chromatography on Sephadex G-150 it was shown that the process was accompanied by a significant decrease in the number of inactive proteins.
D015096:3-Hydroxysteroid Dehydrogenases / Q000302:isolation & purification*; D000327:Adsorption; D001639:Bicarbonates / Q000494:pharmacology; D002411:Cation Exchange Resins / Q000494:pharmacology*; D002789:Cholesterol Oxidase / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D007475:Ion Exchange Resins / Q000494:pharmacology*; D013302:Streptomyces / Q000201:enzymology*
D001639:Bicarbonates; D002411:Cation Exchange Resins; D007475:Ion Exchange Resins; D015096:3-Hydroxysteroid Dehydrogenases; D002789:Cholesterol Oxidase
Ionoobmennaia khromatografiia kholesterinoksidazy iz Actinomyces lavendulae na karboksil'nom kationite tipa Biokarb.