doi: 10.1111/j.1432-1033.1977.tb11424.x.
The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria
- PMID: 15840
- DOI: 10.1111/j.1432-1033.1977.tb11424.x
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The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria
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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