脂蛋白脂酶
乳糜微粒
甘油三酯
载脂蛋白B
脂蛋白
化学
生物化学
甘油三酯脂肪酶
脂肪酶
极低密度脂蛋白
内分泌学
酶
内科学
生物
胆固醇
医学
作者
Yôko Nakaya,Ernst J. Schaefer,H. Bryan Brewer
标识
DOI:10.1016/0006-291x(80)91595-8
摘要
Lipoprotein lipase (LPL) is the major enzyme involved in triglyceride hydrolysis of lymph chylomicrons and plasma very low density lipoproteins. LPL can be isolated from human post heparin plasma by heparin-Sepharose 4B affinity chromatography. In the present study the effects of apolipoproteins (apo) C-II, C-III, and H on the enzymic activity of LPL were investigated. ApoH is a recently described protein (β2-glycoprotein I) constituent of triglyceride rich lipoproteins in human lymph and plasma. Human LPL was activated by apoC-II, and the apoC-II activation of LPL was inhibited by apoC-III. ApoH increased the enzymic activity of LPL in the presence of apoC-II by 45±17 percent. ApoC-III decreased the apoH + apoC-II enhanced activity of LPL by 77 percent. These results provide evidence for the concept that the enzymic activity of LPL in triglyceride metabolism is modulated by apoH. The relative proportion of apoH, apoC-II, and apoC-III in triglyceride rich lipoprotein particles may determine the ultimate rate of LPL catalyzed triglyceride hydrolysis.
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