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  • Title: Temperature dependence of membranous and solubilized sialyltransferase activities in the presence of 1-palmitoyl-sn-glycero-3-phosphorylcholine and fatty acids.
    Author: Bador H, Morelis R, Louisot P.
    Journal: Biochimie; 1984 Mar; 66(3):223-33. PubMed ID: 6743698.
    Abstract:
    The temperature dependence of sialyltransferase (CMP-N-acetylneuraminate: D-galactosyl-glycoprotein N-acetyl-neuraminyltrasferase, EC 2.4.99.1) inhibition is described when 1-palmitoyl-sn-glycero-3-phosphorylcholine, or a saturated fatty acid (lauric, myristic or palmitic acid) or an equimolar mixture of the two components are added. Lysophospholipid and fatty acids have no appreciable effect on the optimal temperature for sialyltransferase activity. In the presence of lysophospholipid, the membranous sialyltransferase activity is decreased for all the temperature range tested. In contrast, the solubilized sialyltransferase activity is decreased for temperatures exceeding 29 degrees C. In the presence of saturated fatty acids, the membranous activity is decreased above a chain-length dependent temperature: 22 degrees, 25 degrees and 30 degrees C for lauric, myristic and palmitic acids, respectively. In contrast, the solubilized activity remains unchanged. In the presence of equimolar mixtures of lysophospholipid and fatty acid, the membranous activity is decreased above the same critical temperature as that described for fatty acids added alone. In contrast, the solubilized activity is decreased above 29 degrees C. From these observations, it is suggested that lysophospholipid inhibits the solubilized enzyme when the temperature exceeds the critical micellar temperature of this lipid. The fatty acids inhibit the microsomal enzyme probably by incorporating into the membrane. It is also suggested that equimolar mixtures of lysophospholipid and fatty acid give rise to molecular analogs of 1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine.
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