Etienne J, Breton M, Vanhove A, Polonovski J
Biochim Biophys Acta. 1976 Mar 11;429(1):198-204. doi: 10.1016/0005-2744(76)90042-5.
Lipoprotein lipase (EC 3.1.1.3) from rat adipose tissue was purified by affinity chromatography with heparin-Sepharose. Elution was carried out with buffered solutions of increasing NaCl molarity. Proteins without affinity for heparin were eluted with 0.5 M NaCl, while lipoprotein lipase activity was eluted as two peaks with 1.16 M NaCl (In earlier work on human adipose tissue (Etienne et al. (1974) C.R. Acad. Sc. Paris 279, 1487-1490) two fractions with lipoprotein lipase activity were also obtained). Phospholipase activity was detected in the fraction eluted with buffered 0.5 M NaCl and containing proteins without affinity for heparin. On feeding the fasting rats with fresh cream or glucose two peaks were also obtained, but the first peak had clearly increased while the second one had remained virtually unchanged.
采用肝素-琼脂糖亲和层析法对大鼠脂肪组织中的脂蛋白脂肪酶（EC 3.1.1.3）进行纯化。用NaCl摩尔浓度递增的缓冲溶液进行洗脱。对肝素无亲和力的蛋白质用0.5 M NaCl洗脱，而脂蛋白脂肪酶活性以两个峰的形式在1.16 M NaCl时被洗脱（在早期关于人类脂肪组织的研究中（艾蒂安等人（1974年）《法国科学院院报》279，1487 - 1490），也获得了具有脂蛋白脂肪酶活性的两个组分）。在用0.5 M NaCl缓冲液洗脱且含有对肝素无亲和力的蛋白质的组分中检测到了磷脂酶活性。给禁食大鼠喂食鲜奶油或葡萄糖后也得到了两个峰，但第一个峰明显增加，而第二个峰几乎保持不变。
