Biosynthesis and Secretion of Milk / Diseases by Bruce L. Larson

By Bruce L. Larson

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However, caution must be exerted in the intepretation of the low acetyl-CoA carboxylase activities because of the difficulties encountered in assaying this enzyme. The in vitro assay requires activation of acetylCoA carboxylase to the polymeric form for maximum activity. The regulatory role postulated for acetyl-CoA carboxylase in mammary fatty acid synthesis is supported by the changes which occur in the activity of this enzyme at the initiation of lactation and at involution. 97 between acetyl-CoA carboxylase activity and lipogenic capacity of the tissue as measured by in vitro incubations ( Mellenberger et al, 1973 ).

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Advan. Lipid Res. 9, 1. Tove, S. B. (1965). In "Physiology of Digestion in the Ruminant" (R. W. ), p. 399. C. Turkington, R. , and Topper, Y. J. (1966). Biochim. Biophys. Ada 127, 366. , and Peeters, G. (1965). Biochem. J. 94, 183. Verley, J. , and Hollmann, K. H. (1966). Z. Zellforsch. Mikrosk. Anat. 75, 605. Wagner, R. , and Cynkin, M. A. (1971). /. Biol. Chem. 246, 143. Wakil, S. J. (1962). Ann. Rev. Biochem. 31, 369. , and McLean, P. (1968). Biochem. J. 109, 737. Wise, E. , and Ball, E. G. (1964).

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