Abstract
Palmityl-coenzyme A: L-α-glycerolphosphate acyltransferase is the most active acyltransferase of bovine mammary microsomes, with a specific activity ranging from 8–20 nmoles min−1 mg−1 protein. Corresponding acylation rates of 2.2, 1.4, 2.1, and 0.6 nmoles min−1 mg−1 were obtained for myristyl-, stearyl-, oleyl- and linoleyl-coenzyme A, respectively. Optimum pH of palmityltransferase was 7.7, and activity was not affected by buffer molarity in range 25–150 mM. Inhibitory effects of palmityl-coenzyme A (10 μM/0.1 mg microsomal protein) was relieved by bovine serum albumin. Sonication magnesium and ethylenediaminetetraacetic acid enhanced activity. Delipidation of microsomes reduced activity by 84%; restoration of extracted lipids achieved 70% of original activity. Apparent Km and Vmax values of 4.1 and 260 μM and 9.5 and 8.2 nmole min−1 mg−1 were determined for palmityl-coenzyme A and D,L-α-glycerolphosphate, respectively, using untreated microsomes. The enzyme was stable as lyophilized microsomes when stored at −30 C. Phosphatidic acid was the major product and marked quantities of diglycerides were formed, especially when microsomal protein was increased.
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Gross, M.J., Kinsella, J.E. Properties of palmityl-CoA: L-α-glycerolphosphate acyl transferase from bovine mammary microsomes. Lipids 9, 905–912 (1974). https://doi.org/10.1007/BF02532617
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DOI: https://doi.org/10.1007/BF02532617