Cholinephosphotransferase activity in human platelets

descriptionPublicationkeyboard_double_arrow_right Article 01 Mar 1983 Italy English Publisher:WileyJournal:Lipids, volume 18, pages 179-185 (issn: 0024-4201, eissn: 1558-9307,

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Authors: GORACCI, Gianfrancesco; GRESELE, Paolo; ARIENTI, Giuseppe; P. Porrovecchio; NENCI, Giuseppe Giorgio; PORCELLATI, Giuseppe;

doi: 10.1007/bf02534545

pmid: 6304446

handle: 11391/909601

Cholinephosphotransferase activity in human platelets

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Abstract

AbstractDisrupted human platelets possess a cholinephosphotransferase activity (EC 2.7.8.2) whose properties have been studied in this work. The labeling of choline glycerophospholipid (CGP) from radioactive cytidine‐5′‐diphosphate choline (CDP‐choline) in vitro shows a maximum at pH 8.0 (using Hepes [4‐(2‐hydroxyethyl)‐piperazine‐1‐ethane‐2‐sulfonic acid] as a buffer) and is stimulated by Mn2+, Mg2+ and diacylglycerol. The enzymic activity is inhibited by Ca2+. The dependence of human platelet choline‐phosphotransferase upon CDP‐choline concentration does not follow the Michaelis‐Menten equation. CMP strongly inhibits the reaction. The functional implications of this newly discovered platelet activity are briefly considered.

Country

Italy

Related Organizations

University of Perugia
Italy

Keywords

Blood Platelets, Chemical Phenomena, Cations, Divalent, Phosphotransferases, Blood Proteins, Hydrogen-Ion Concentration, Diglycerides, Enzyme Activation, Chemistry, Diacylglycerol Cholinephosphotransferase, Humans

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