Purification and partial characterization of acetyl-coA synthetase in rat liver mitochondria.

J Nutr Sci Vitaminol (Tokyo)

Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University, 111 Kuboki, Soja, Okayama 719-1197, Japan.

Published: October 2002

Acetyl-CoA synthetase (AceCS), which catalyzes the activation of acetate to produce acetyl-CoA, was found to have a much greater Km value for acetate in liver mitochondria than that in the heart mitochondria of rats, indicating that two different types of AceCS are located in the liver and heart mitochodria. Recently, Fujino et al. reported that mouse heart mitochondrial AceCS, designated AceCS2, was expressed in a wide range of tissues, however, it was apparently absent from the liver. In this study, liver mitochondrial AceCS activity, but not heart AceCS2, was greatly induced in di(2-ethylhexyl)phthalate (DEHP)-treated rats. We purified and characterized the rat liver mitochondrial AceCS. The molecular mass of the enzyme estimated by SDS-PAGE was -58 kDa, which was quite different from that of the heart mitochondrial enzyme, AceCS2. The calculated Km value for the acetate of the partially purified liver enzyme was much greater, being about 100 times that of heart enzyme, AceCS2.

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http://dx.doi.org/10.3177/jnsv.48.359DOI Listing

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