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A 31 P nuclear magnetic resonance investigation of acyl group transfer from phosphatidylcholine to yield lysophosphatidylcholine in human plasma
Author(s) -
NouriSorkhabi M. Hossein,
Sullivan David R.,
Roberts David C.,
Kuchel Philip W.
Publication year - 1994
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536727
Subject(s) - chemistry , phosphatidylcholine , lysophosphatidylcholine , lecithin , nuclear magnetic resonance spectroscopy , acyl group , phospholipid , cholesteryl ester , yield (engineering) , cholesterol , chromatography , biochemistry , lipoprotein , stereochemistry , organic chemistry , alkyl , membrane , materials science , metallurgy
31 P nuclear magnetic resonance (NMR) spectroscopy was used to measure the rate of acyl transfer from phosphatidylcholine (lecithin, PC) in whole plasma and in high density lipoprotein (HDL). Spectral deconvolution was used to resolve overlapping resonances in the 31 P NMR spectra of the phospholipids. Mean values of the acyl group transfer rates from PC in plasma and HDL were 36 μmol L −1 h −1 and 19 μmol L −1 h −1 , respectively. The reciprocal nature of the decrease in the spectral peak intensities of PC, compared to the increase in the intensities of the lysolecithin (lysoPC) peaks, suggested a substrate/product relationship consistent with the action of lecithin:cholesterol acyltransferase (LCAT), the enzyme responsible for the esterification of free cholesterol in plasma. LCAT involvement was confirmed by measuring the cholesterol esterification rate based on the 13 C NMR spectra obtained on lipid extracts from plasma that had been incubated at 37°C. Within experimental error, the rate of lysoPC formation in plasma was shown to be equal to that of cholesteryl ester formation.