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Monoacyl‐ sn ‐glycerol 3‐phosphate acyltransferase specificity in bovine mammary microsomes
Author(s) -
Kinsella John E.
Publication year - 1976
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532886
Subject(s) - acylation , phosphatidic acid , chemistry , microsome , acyltransferases , acyltransferase , phosphate , glycerol , clinical chemistry , chromatography , biochemistry , phospholipid , enzyme , biosynthesis , catalysis , membrane
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.