Purification and partial characterisation of NADP(+)-linked isocitrate dehydrogenase from rat liver cytosol.
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.
Fatania
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Department of Biochemistry, Faculty of Medicine, Kuwait University.
al-Nassar
K E
KE
Sidhan
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V
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
D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+)