Studies on the degradation of human very low density lipoproteins by human milk lipoprotein lipase.
Studies on the degradation of human very low density lipoproteins by human milk lipoprotein lipase.
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人乳脂蛋白脂肪酶降解人极低密度脂蛋白的研究。
DOI：
10.1016/0003-9861(82)90004-2
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发表时间：
1982
影响因子：
3.9
通讯作者：
W. Mcconathy
中科院分区：
文献类型：
--
作者：
C. S. Wang;D. Weiser;P. Alaupovic;W. Mcconathy
人乳脂蛋白脂肪酶（LPL）通过肝素-Sepharose 4B 亲和层析纯化。纯化所需的时间约为2小时。用0.1% Triton X-100缓冲溶液提取奶油的丙酮-乙醚粉末，并将提取物上样至肝素-Sepharose 4B柱。肝素洗脱的部分纯化的LPL具有5120单位/mg的比活性，这代表酶的2500倍纯化。发现 LPL 在 4 °C 的肝素溶液中稳定至少 2 天。发现该酶制剂不含胆汁盐激活的脂肪酶活性、酯酶活性和胆固醇酯酶活性。在没有血清辅因子的情况下，LPL 与乳化三油酸甘油酯没有明显的基础活性。该酶被血清和载脂蛋白 C-II 激活。应用牛奶 LPL 进行人类极低密度脂蛋白体外降解研究，可导致 90-97% 的甘油三酯水解。 LPL 降解极低密度脂蛋白甘油三酯和磷脂，对胆固醇酯没有任何影响。在用牛奶 LPL 脂解可能产生的偏甘油酯中，在脂解 60 分钟后，只有单甘油酯以可测量的量存在。这些结果表明，部分纯化的母乳LPL具有高比活性和易于纯化的特点，是一种非常适合研究富含甘油三酯的脂蛋白的脂解降解动力学和反应机制的酶制剂。
Human milk lipoprotein lipase (LPL) was purified by heparin-Sepharose 4B affinity chromatography. The time required for the purification was approximately 2 h. The acetone-diethyl ether powder of milk cream was extracted by a 0.1% Triton X-100 buffer solution and the extract was applied to the heparin-Sepharose 4B column. The partially purified LPL eluted by heparin had a specific activity of 5120 units/mg which represented a 2500-fold purification of the enzyme. The LPL was found to be stable in the heparin solution for at least 2 days at 4 °C. This enzyme preparation was found to be free of the bile salt-activated lipase activity, esterase activity, and cholesterol esterase activity. The LPL had no demonstrable basal activity with emulsified triolein in the absence of a serum cofactor. The enzyme was activated by serum and by apolipoprotein C-II. The application of milk LPL to studies on thein vitrodegradation of human very low density lipoproteins can result in a 90–97% triglyceride hydrolysis. The LPL degraded very low density lipoprotein triglyceride and phospholipid without any effect on cholesterol esters. Of the partial glycerides potentially generated by lipolysis with milk LPL, only monoglycerides were present in measurable amounts after 60 min of lipolysis. These results show that the partially purified human milk LPL with its high specific activity and ease of purification represents a very suitable enzyme preparation for studying the kinetics and reaction mechanisms involved in the lipolytic degradation of human triglyceride-rich lipoproteins.
血浆磷脂转移蛋白增强脂解过程中极低密度脂蛋白和高密度脂蛋白之间磷脂的转移和交换。
影响因子：
6.5
作者：
Tall,AR;Krumholz,S;Olivecrona,T;Deckelbaum,RJ
通讯作者：
Deckelbaum,RJ