1,2-diacylglycerol kinase of human erythrocyte membranes. Assay with endogenously generated substrate.
1,2-Diacylglycerol kinase activity was measured in human erythrocyte membranes using an assay procedure in which the substrate was generated endogenously, either by treatment with a bacterial phospholipase C or by incubation with Ca24, which activates a membrane-bound polyphosphoinositide phosphodiesterase. The properties of 1,2-diacylglycerol kinase were broadly similar to those described previously, except that in the present work maximum activities were higher and there was evidence for a double pH optimum.
D002118:Calcium / Q000494:pharmacology; D019852:Diacylglycerol Kinase; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010712:Phosphatidic Acids / Q000096:biosynthesis; D010770:Phosphotransferases / Q000097:blood*; D010738:Type C Phospholipases / Q000494:pharmacology
D010712:Phosphatidic Acids; D010770:Phosphotransferases; D019852:Diacylglycerol Kinase; D010738:Type C Phospholipases; D002118:Calcium