Apoc-III-beta-galactosidase hybrid distinguishes between VLDL and LDL phospholipids.
A plasmid directing the expression of preapolipoprotein C-III fused to beta-galactosidase was constructed. Escherichia coli harboring this construct produced the hybrid, with full beta-galactosidase activity, at 0.6% of total cellular protein. Purified preapoC-III-beta-galactosidase hybrid exhibited specific binding to very low density lipoproteins, which was inhibited by purified apoC-III. No binding to low density lipoproteins was observed. Binding was mediated by the phospholipids of very low density lipoproteins, as the hybrid had a specific affinity for phospholipids and no detectable affinity for triglycerides, cholesteryl esters, or cholesterol. The differential binding suggests that there are differences between the phospholipids of very low density lipoproteins and the phospholipids of low density lipoproteins.
Trieu
V N
VN
Department of Medicine, University of North Texas Health Science Center at Fort Worth 76107, USA.
McConathy
W J
WJ
D000595:Amino Acid Sequence; D053305:Apolipoprotein C-III; D001056:Apolipoproteins C / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D008074:Lipoproteins; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008079:Lipoproteins, VLDL / Q000378:metabolism*; D008969:Molecular Sequence Data; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D001616:beta-Galactosidase / Q000235:genetics
D053305:Apolipoprotein C-III; D001056:Apolipoproteins C; D008074:Lipoproteins; D008077:Lipoproteins, LDL; D008079:Lipoproteins, VLDL; D010743:Phospholipids; D011498:Protein Precursors; D011993:Recombinant Fusion Proteins; D001616:beta-Galactosidase