1,2-diacylglycerol kinase of human erythrocyte membranes. Assay with endogenously generated substrate

D ALLAN; P THOMAS; S GATT

doi:10.1042/bj1910669

1,2-diacylglycerol kinase of human erythrocyte membranes. Assay with endogenously generated substrate

D ALLAN, P THOMAS, S GATT

Faculty of Science

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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.

Original language	English
Pages (from-to)	669–672
Number of pages	4
Journal	Biochemical Journal
Volume	191
Issue number	2
DOIs	https://doi.org/10.1042/bj1910669
Publication status	Published - 1 Nov 1980

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10.1042/bj1910669

Cite this

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title = "1,2-diacylglycerol kinase of human erythrocyte membranes. Assay with endogenously generated substrate",

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.",

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AU - ALLAN, D

AU - THOMAS, P

AU - GATT, S

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N2 - 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.

AB - 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.

U2 - 10.1042/bj1910669

DO - 10.1042/bj1910669

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JO - Biochemical Journal

JF - Biochemical Journal

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