[Isolation and purification of NADP-dependent "L-malate"-enzyme from corn leaves].
Persanov Vm, E A Voronova, L A Oparina, Iu S Karpilov
Abstract
Persanov Vm, E A Voronova, L A Oparina, Iu S Karpilov
Abstract
Isolation and purification of "malic-enzyme" NADP was done using fractionation by ammonium sulfate, anion-exchange chromatography on DEAE cellulose, gel-filtration through Sephadex G-200 and purification on DEAE Sephadex A-50. The isoenzyme isolated had a specific activity of 40-50 mkM/mg protein per min (approximately 80-fold purification) and contained negligible admixtures.
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Isolation and purification of "malic-enzyme" NADP was done using fractionation by ammonium sulfate, anion-exchange chromatography on DEAE cellulose, gel-filtration through Sephadex G-200 and purification on DEAE Sephadex A-50. The isoenzyme isolated had a specific activity of 40-50 mkM/mg protein per min (approximately 80-fold purification) and contained negligible admixtures.
Key concepts: Sephadex, Size-exclusion chromatography, Chromatography, Fractionation, Chemistry, Ammonium sulfate, Malic enzyme, Enzyme