Demonstration of enzymatic conversion of lysolecithin to lecithin in normal human plasma
An enzyme in normal human plasma that converts [1-acyl 14C] lysolecithin to lecithin is demonstrated. This enzyme is inhibited by heparin and is not derived from platelets or other blood elements. The synthesis of lecithin from labeled lysolecithin was not stimulated by ATP and CoA or by oleyl CoA a...
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Veröffentlicht in: | Life sciences (1973) 1978-06, Vol.22 (22), p.1971-1977 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | An enzyme in normal human plasma that converts [1-acyl
14C] lysolecithin to lecithin is demonstrated. This enzyme is inhibited by heparin and is not derived from platelets or other blood elements. The synthesis of lecithin from labeled lysolecithin was not stimulated by ATP and CoA or by oleyl CoA and there was nearly an equal distribution of labeled fatty acid between the two positions of lecithin indicating that the enzyme may be a lysolecithin: lysolecithin acyl transferase (LLAT). The enzyme is associated with the lipoproteins of the plasma, and may have a physiological role in the formation of saturated cholesterol esters in plasma. |
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ISSN: | 0024-3205 1879-0631 |
DOI: | 10.1016/0024-3205(78)90541-6 |