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January 1, 1985Journal of Biological ChemistryOpen Access

Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.

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Authors

YIYasuyuki IkedaNational Cerebral and Cardiovascular CenterKOKazuko Okamura‐IkedaTokushima UniversityKTKay TanakaYale University

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Cite This Study

Ikeda et al. (1985) studied this question.

synapsesocial.com/papers/6a88f6cbc9c00c271ba2a418https://doi.org/10.1016/s0021-9258(20)71245-7
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  1. 1Purification and characterization of 2-methyl-branched chain acyl coenzyme A dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria.1983 · 109 citations
  2. 2Dicarboxylic Aciduria: Deficient [1- <sup>14</sup> C]Octanoate Oxidation and Medium-Chain Acyl-CoA Dehydrogenase in Fibroblasts1983 · 109 citations
  3. 3Purification and Properties of Rat Liver Acyl-CoA Dehydrogenases and Electron Transfer Flavoprotein11981 · 129 citations