Purification and properties of the nicotinamide-adenine dinucleotide phosphate-dependent isocitrate dehydrogenase from pig liver cytoplasm.
The NADP-dependent isocitrate dehydrogenase from pig liver soluble fraction was purified over 500-fold with an overall yield of 25%. The purified enzyme, which is homogeneous by all the usual criteria, has a molecular weight of about 75000 and is composed of two identical subunits. This has been demonstrated by ultracentrifugation, fluorescence titration and peptide ;fingerprinting'. The maximal turnover number, extinction coefficients at 280nm and 260nm and amino acid analysis are described.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002247:Carbon Isotopes; D002855:Chromatography, Thin Layer; D003593:Cytoplasm / Q000201:enzymology*; D004586:Electrophoresis; D005453:Fluorescence; D007521:Isocitrate Dehydrogenase / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009249:NADP; D010455:Peptides / Q000302:isolation & purification; D013552:Swine; D014461:Ultracentrifugation
D000596:Amino Acids; D002247:Carbon Isotopes; D010455:Peptides; D009249:NADP; D007521:Isocitrate Dehydrogenase