Simultaneous transfer of cholesteryl ester and phospholipid by protein(s) isolated from human lipoprotein-free plasma |
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Authors: | Jahei Ihm Judith A.K. Harmony Jeff Ellsworth Richard L. Jackson |
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Affiliation: | 1. Division of Lipoprotein Research, Department of Pharmacology and Cell Biophysics, University of Cincinnati Medical Center, Cincinnati, Ohio 45267 USA;2. Department of Biological Chemistry, University of Cincinnati Medical Center, Cincinnati, Ohio 45267 USA;3. Department of Medicine, University of Cincinnati Medical Center, Cincinnati, Ohio 45267 USA |
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Abstract: | Protein(s) catalyzing the transfer of [3H]cholesteryl ester and [14C]-phosphatidylcholine from high density lipoproteins to low density lipoproteins have been purified 4829-fold from human plasma by chromatography of the d > 1.21 g/ml infranatant fraction of human plasma on phenyl-Sepharose, CM-cellulose, concanavalin A-Sepharose, and finally by isoelectric focussing. At each step of the purification, both transfer activities coelute. The purified protein(s), molecular weight 150,000, transfer cholesteryl esters and phosphatidylcholine with a 1:1 stoichiometry and at equal rates of flux. Rat plasma contains a protein(s) which facilitates the transfer of phosphatidylcholine as effectively as human plasma. However, the rat plasma protein(s) does not facilitate the transfer of cholesteryl esters. These results suggest that human plasma contains one or more proteins which transfer both lipids, possibly as a 1:1 complex, whereas rat plasma lacks the cholesteryl ester transfer protein. |
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