| Literature DB >> 6263251 |
Abstract
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.Entities:
Mesh:
Substances:
Year: 1980 PMID: 6263251 PMCID: PMC1162263 DOI: 10.1042/bj1910669
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857