Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein
WV Brown, ML Baginsky - Biochemical and biophysical research …, 1972 - Elsevier
WV Brown, ML Baginsky
Biochemical and biophysical research communications, 1972•ElsevierThe 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 …
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 …
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.
Elsevier