Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein.
Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein.
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DOI：
10.1016/s0006-291x(72)80149-9
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发表时间：
1972-01
影响因子：
3.1
通讯作者：
W. Brown;M. Baginsky
中科院分区：
文献类型：
--
作者：
W. Brown;M. Baginsky
本文研究了从人极低密度脂蛋白中分离的两种载脂蛋白（apoLp-Glu和apoLp-Ala）对脂蛋白脂酶（LPL）活性的影响。ApoLp-Glu显著刺激LPL。通过先前描述的技术分离的ApoLp-Ala也以低水平激活LPL。然而，通过羟基磷灰石色谱进一步纯化，通过去除与apoLp-Glu免疫化学相同的小污染物，消除了apoLp-Ala的所有活化。当以高于底物的2%（w/w）的水平存在时，ApoLp-Ala始终抑制LPL。加入磷脂、apoLp-Glu或更多的酶不能克服这种抑制作用。
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.