The Purification and Properties of NADP‐Dependent Isocitrate Dehydrogenase from Ox‐Heart Mitochondria
Open Access
- 1 April 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 74 (3) , 553-559
- https://doi.org/10.1111/j.1432-1033.1977.tb11424.x
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, A2801% estimated from dry weight measurements is 11.8 cm−1.This publication has 30 references indexed in Scilit:
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