1. Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein
- Author
-
W. Virgil Brown and M.L. Baginsky
- Subjects
Very low-density lipoprotein ,Apolipoprotein C ,Lipoproteins ,Apolipoprotein C-II ,Guinea Pigs ,Biophysics ,Phospholipid ,Hyperlipidemias ,Biochemistry ,chemistry.chemical_compound ,Animals ,Humans ,Molecular Biology ,Phospholipids ,Intermediate-density lipoprotein ,Carbon Isotopes ,Chromatography ,Lipoprotein lipase ,Chemistry ,Immune Sera ,Apolipoprotein C-III ,Blood Proteins ,Cell Biology ,Enzyme Activation ,Lipoprotein Lipase ,Milk ,Apolipoprotein C-I ,Cattle ,lipids (amino acids, peptides, and proteins) ,Hydroxyapatites - Abstract
Summary The effects of two apolipoproteins isolated from human very low density lipoproteins (apoLp-Glu and apoLp-Ala) on lipoprotein lipase (LPL) activity have been studied. ApoLp-Glu markedly stimulated LPL as reported by others. ApoLp-Ala isolated by techniques previously described also activated LPL at low levels. However, with further purification by hydroxylapatite chromatography all activation by apoLp-Ala was eliminated with the removal of a small contaminant immunochemically identical to apoLp-Glu. ApoLp-Ala consistently inhibits LPL when present at levels above 2% of the substrate (w/w). This inhibition was not overcome by addition of phospholipid, apoLp-Glu, or more enzyme.
- Published
- 1972