Abstract
The acyl‐CoA∶:acyl‐sn‐glycerol 3‐phosphate acyltransferases located in the microsomal fraction of lactating bovine mammary tissue show a preference for palmityl‐CoA particularly above the apparent Km values of the acyl acceptors. Using saturating levels of monopalmityl‐sn‐glycerol 3‐phosphate, the order of acylation was palmityl‐>myristyl‐> oleyl‐>stearyl‐>linoleyl‐CoA. Apparent Km values for monopalmityl‐ and monooleyl‐sn‐glycerol 3‐phosphate with palmityl‐CoA as donor were 16 and 13μM, respectively, while the Km values for palmityl‐CoA with these two acyl acceptors were 5 and 5.2μM, respectively. The apparent Vmax values for the palmityl acceptor and donor were 25 and 30 nmol/min/mg protein. Phosphatidic acid was the principal product. The inclusion of magnesium in the assay depressed activity while the addition of ethylenediaminetetraacetate doubled the rate of acylation.

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