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J. Biochem, 1984, Vol. 96, No. 5 1463-1469
© 1984 Japanese Biochemical Society

research-article

Studies on the Metabolism of Unsaturated Fatty Acids. XV. Purification and Properties of 2,4-Dienoyl-CoA Reductase from Rat Liver Peroxisomes1

Chiharu KIMURA*, Akira KONDO*, Noriko KOEDA*, Hiroshi YAMANAKA* and Michinao MIZUGAKI**,2

*Pharmaceutical Institute, Tohoku University, Aobayama Sendai, Miyagi 980
**Department of Pharmaceutical Sciences, Tohoku University Hospital Sendai, Miyagi 980

2 To whom correspondence should be addressed

Peroxisomal 2,4-dienoyl-CoA reductase was purified from rat liver to homogeneity. The subunit molecular weight of 33,000 was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The native molecular weight close to 120,000 was estimated by gel filtration on Sephacryl S-300 Superfine. trans-2, trans-4-Decadienoyl-CoA was the most active substrate among the dienoyl-CoA's of various chain lengths. The total activity of peroxisomal 2,4-dienoyl-CoA reductase exceeded that of the mitochondrial one even in the livers of rats fed with a standard diet. Furthermore both reductases were remarkably and coordinately induced in the livers of clofibrate-treated rats.

1 Part XIV: Studies on the Metabolism of Unsaturated Fatty Acids. XIV. Purification and Properties of NADPH-dependent trans-2-Enoyl-CoA Reductase of Escherichia coli K-12. Nishimaki, T., Yamanaka, H., & Mizugaki, M. (1984) J. Biochem. 95, 1315–1321.


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