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. 1977 Apr 15;74(3):553-9.
doi: 10.1111/j.1432-1033.1977.tb11424.x.

The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria

N Macfarlane, B Mathews, K Dalziel
Free article

The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria

N Macfarlane et al. Eur J Biochem. .
Free article

Abstract

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.

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