人乳和牛乳脂蛋白脂肪酶的动力学以及载脂蛋白C-II对酶的激活机制。
Kinetics of human and bovine milk lipoprotein lipase and the mechanism of enzyme activation by apolipoprotein C-II.
作者信息
Posner I, Wang C S, McConathy W J
出版信息
Comp Biochem Physiol B. 1985;80(1):171-4. doi: 10.1016/0305-0491(85)90441-9.
The kinetics of human and bovine milk lipoprotein lipase (HM-LPL and BM-LPL, respectively) were compared by varying apolipoprotein C-II (C-II) or triacylglycerol (TG) concentrations. The apparent Km (TG) and Km (C-II) for HM-LPL were 2.2 and 6.7-fold higher than for BM-LPL. Plots of 1/v vs 1/[TG] or 1/[C-II] intercepted the respective abscissas at the same points: C-II had no effect on Km (TG) and TG had no effect on Km (C-II). Replots of slope 1/s vs 1/[C-II] gave straight lines which yielded KA values identical to Km (C-II). It is concluded that the HM-LPL system follows a random, bireactant, rapid equilibrium mechanism as shown previously for BM-LPL.
通过改变载脂蛋白C-II（C-II）或三酰甘油（TG）的浓度，比较了人乳和牛乳脂蛋白脂肪酶（分别为HM-LPL和BM-LPL）的动力学。HM-LPL的表观Km（TG）和Km（C-II）分别比BM-LPL高2.2倍和6.7倍。1/v对1/[TG]或1/[C-II]的曲线在相应横坐标的同一点相交：C-II对Km（TG）无影响，TG对Km（C-II）无影响。斜率1/s对1/[C-II]的重新作图得到直线，其KA值与Km（C-II）相同。结论是，HM-LPL系统遵循随机、双反应物、快速平衡机制，如先前对BM-LPL所示。
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