title: Purification and partial characterisation of NADP(+)-linked isocitrate dehydrogenase from rat liver cytosol.
abstract: NADP(+)-linked isocitrate dehydrogenase from rat liver cytosol was purified (approximately 135-fold) to apparent homogeneity in 27% yield. The purified enzyme has specific activity of 73 units.mg-1. The native enzyme showed an apparent M(r) of 94,000 by gel filtration and was composed of two identical subunits of M(r) 45,000 as judged by SDS/PAGE. In isoelectric focusing, a pI value of 5.7 was estimated for the enzyme.
authors: Department of Biochemistry, Faculty of Medicine, Kuwait University.
authors: H
authors: H
authors: Fatania
authors: K E
authors: KE
authors: al-Nassar
authors: V
authors: V
authors: Sidhan
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007521:Isocitrate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D017208:Rats, Wistar
chemical_list: D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+)