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Partial Purification of Enzymes of Bovine Kidney Mitochondria Activating Volatile Fatty Acids^{1 ,2,}

Department of Dairy Science, Michigan State University, East Lansing 48824

ABSTRACT

Mitochondria were prepared from kidney cortex tissue of lactating Holstein cows, and enzymes activating volatile fatty acids partially purified. Two fractions activating volatile fatty acids were obtained; one was similar to components isolated from bovine heart mitochondria activating acetate and propionate (acetyl CoA synthetase). The other was similar to components of bovine liver mitochondria and activated propionate, butyrate, and valerate but not acetate. On calcium phosphate gel chromatography this latter fraction could be separated into a distinct propionyl CoA synthetase (Michaelis-Menten constant for propionate 2.54 x 10^–3 M) and a fraction activating butyrate and valerate. The role of a distinct propionyl CoA synthetase in kidney mitochondria remains to be elucidated because propionate is not a major substrate in peripheral blood of ruminants.

We concluded that volatile fatty acid activation by bovine kidney mitochondria is due to an acetyl CoA synthetase, a propionyl CoA synthetase, and a butyrate and valerate-activating fraction probably composed of separate butyryl and valeryl CoA synthetases.

¹ Published with approval of the Director of the Agricultural Experiment Station as Journal Article No. 4905.

² Data taken from dissertation by senior author in partial fulfillment of the requirements for the Ph.D. degree.

³ American Cyanamid Company, P. O. Box 400, Princeton, NJ 08540.