Abstract
1,2-Diacylglycerol kinase activity was measured in human erythrocyte membranes using an assay procedure in which the substrate was generated endogenuously, either by treatment with a bacterial phospholipase C or by incubation with Ca2+, 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.
Original language | English |
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Pages (from-to) | 669-672 |
Number of pages | 4 |
Journal | Biochemical Journal |
Volume | 191 |
Issue number | 2 |
DOIs | |
State | Published - 1980 |
Externally published | Yes |