Mitamura T, Imai Y
Hokkaido Igaku Zasshi. 1977 Jul;52(4):359-64.
The effect of calcium on the activation of lipoprotein lipase by heparin was studied using ammonia buffer extracts of acetone powder from guinea pig adipose tissue as the lipoprotein lipase source. Lipase activity was assayed with an artificial triglyceride emulsion that had been activated with rat high density lipoproteins. The addition of Ca2+ (2mM) alone increased the lipoprotein lipase activity about 2.5- to 3.5-fold, but heparin (1 unit/ml) alone had little effect. When both Ca2+ and heparin were added to the assay medium, the activity was increased to 4- to 5- fold above control values. When Ca2+ in the assay medium was sequestrated by EGTA, these increases by Ca2+ and heparin were completely abolished. The results suggest that the presence of Ca2+ is a prerequisite for the activation of lipoprotein lipase by heparin. Gel filtration of the mixture of acetone poder extracts and [3H] heparin showed the enzyme bound [3H] heparin whether Ca2+ was present or not. In addition to lipoprotein lipase, there were proteins in adipose tissue extracts which had an affinity for heparin.
以豚鼠脂肪组织丙酮粉的氨缓冲液提取物作为脂蛋白脂肪酶来源,研究了钙对肝素激活脂蛋白脂肪酶的作用。用经大鼠高密度脂蛋白激活的人工甘油三酯乳剂测定脂肪酶活性。单独添加Ca2+(2mM)可使脂蛋白脂肪酶活性增加约2.5至3.5倍,但单独添加肝素(1单位/毫升)几乎没有作用。当Ca2+和肝素都添加到测定介质中时,活性增加到对照值以上的4至5倍。当测定介质中的Ca2+被EGTA螯合时,Ca2+和肝素引起的这些增加完全消失。结果表明,Ca2+的存在是肝素激活脂蛋白脂肪酶的先决条件。对丙酮粉提取物和[3H]肝素的混合物进行凝胶过滤,结果显示无论是否存在Ca2+,该酶都能结合[3H]肝素。除脂蛋白脂肪酶外,脂肪组织提取物中还有对肝素有亲和力的蛋白质。