Assay of glycerol phosphate acyltransferase in liver particles

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Abstract
The assay system for glycerol 1-phosphate acyltransferase has been improved by the addition of serum albumin to the reaction system. This causes a shift in the optimum pH to 6.5, depresses palmitoyl-CoA hydrolase and accelerates transferase activity. Serum albumin prevents the inactivation of the transferase brought about by its interaction with palmitoyl-CoA. Free fatty acids, added to the system, inactivate the transferase only at concentrations exceeding those formed during the reaction by a factor of ten.