Partial purification and characterization of an Ls-NADP:isocitrate oxidoreductase from embryonic chick liver Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/gb19f926r

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  • An Ls-isocitrate:NADP oxidoreductase has been isolated and purified from embryonic chicken liver. The enzyme was purified 200 fold by means of ammonium sulfate fractionation, gel filtration chromatography on Sephadex G-200, ion-exchange chromatography on Bio-Gel CM-100 and adsorption chromatography on hydroxylapatite gel. The purified enzyme was nearly homogeneous as determined from sedimentation velocity and sedimentation equilibrium ultracentrifugation. The enzyme had an apparent sedimentation coefficient of about 6.15 S and an apparent molecular weight of approximately 1.15 x 10⁵. The presence of 8 mM isocitrate or 0.42 M ammonium sulfate stabilized the enzyme against inactivation by heating, but did not alter the molecular weight of the enzyme. In the presence of 8mM isocitrate the molecular weight of the enzyme was not altered by an increase in temperature from 4° C to 20 ° C. 0.42 M ammonium sulfate containing 5 mM NADP also did not affect the molecular weight of the enzyme. There was no indication of a chemical equilibrium between the enzyme and an enzyme aggregate. These data indicate that the native supernatant NADP-isocitrate dehydrogenase from embryonic chick liver has a molecular weight of 1. 15 x10⁵ and that stability against heat inactivation is not the result of enzyme aggregation.
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