The Purification and Properties of NADP-Dependent Isocitrate Dehydrogenase from Ox-Heart Mitochondria

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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.

Abbreviation
 

Nbs2+5,5′-dithio-bis(2-nitobenzoic acid)

Enzymes
 

Isocitrate dehydrogenase (EC 1.1.1.42)

 

6-phosphogluamate dehydrogenase (EC 1.1.1.44)

 

glutamate dehydrogenase (EC 1.4.1.3)

 

catalase (EC 1.11.1.6)

 

alcohol dehydrogenase (EC 1.1.1.1)

 

lipoamide dehydrogenase (EC 1.6.4.3)

 

malate dehydrogenase (EC 1.1.1.37)

Ancillary