Monoacyl-sn-glycerol 3-phosphate acyltransferase specificity in bovine mammary microsomes

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- greater than myristyl- greater than oleyl- greater than stearyl- greater than linoleyl-CoA. Apparent Km values for monopalmityl- and mono-oleyl-sn-glycerol 3-phosphate with palmityl-CoA as donor were 16 and 13muM, respectively while the Km values for palmityl-CoA with these two acyl acceptors were 5 and 5.2muM, 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.