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 p I value of 5.7 was estimated for the enzyme.
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