| Literature DB >> 15840 |
N Macfarlane, B Mathews, K Dalziel.
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.Entities:
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Year: 1977 PMID: 15840 DOI: 10.1111/j.1432-1033.1977.tb11424.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956