Cholinephosphotransferase Activity in Human Platelets
Overview
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Disrupted 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 cholinephosphotransferase 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.
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PMID: 8382052 PMC: 1132249. DOI: 10.1042/bj2890815.
Reversibility of cholinephosphotransferase in lung microsomes.
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PMID: 3020334 DOI: 10.1007/BF02535636.
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PMID: 2849012 DOI: 10.1007/BF02536337.