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Title: Purification and positional specificity of sn-glycerol-3-phosphate acyltransferase from Escherichia coli membranes. Author: Ishinaga M, Nishihara M, Kito M. Journal: Biochim Biophys Acta; 1976 Nov 19; 450(2):269-72. PubMed ID: 10989. Abstract: SN-Glycerol-3-phosphate acyltransferase was solubilized from membranes of Escherichia coli B and K-12 and purified on an affinity column of Sepharose 4B coupled with 6-phosphogluconic acid. Phosphatidylglycerol was required for activation and stabilization of the purified enzyme. The acyl residues were exclusively transferred to the position 1 of sn-glycerol 3-phosphate by the enzyme, regardless of whether the acyl-CoA was saturated or unsaturated.[Abstract] [Full Text] [Related] [New Search]