Partial purification of enzymes of bovine kidney mitochondria activating volatile fatty acids [Lactating Holstein cows]

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 p...

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Bibliographic Details
Published in:Journal of dairy science 1981-12, Vol.64 (12), p.2344-2349
Main Author: Ricks, Catherine A
Format: Article
Language:English
Subjects:
Acetate-CoA Ligase - isolation & purification
Animals
cattle
Cattle - metabolism
Chromatography, DEAE-Cellulose
Coenzyme A Ligases - isolation & purification
enzymes
fatty acids
Fatty Acids, Volatile - metabolism
Kidney - enzymology
Kidney - ultrastructure
liver
mitochondria
Mitochondria - enzymology
purification
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Summary: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.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(81)82856-1