PURIFICATION AND POSITIONAL SPECIFICITY OF SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE FROM ESCHERICHIA-COLI MEMBRANES
- 1 January 1976
- journal article
- research article
- Vol. 450 (2) , 269-272
Abstract
Sn-Glycerol-3-phosphate acyltransferase [EC 2.3.1.15] was solubilized from membranes of E. 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.This publication has 6 references indexed in Scilit:
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