The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria.
The purification of NADP-linked isocitrate dehydrogenase from ox heart mitochondria is described. The molecular weight from gel filtration, sedimentation equilibrium and gel electrophoresis is 90000+/-4000, and there are two subunits in the molecule each of which binds NADPH with enhancement of the coenzyme fluorescence. The amino-acid composition is reported, and the absorption coefficient, A1/280%, estimated from dry weight measurements is 11.8 cm-1.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D007521:Isocitrate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008931:Mitochondria, Muscle / Q000201:enzymology*; D008970:Molecular Weight; D009206:Myocardium; D009249:NADP; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D009249:NADP; D014364:Tryptophan; D007521:Isocitrate Dehydrogenase