Jackson R L, Socorro L, Fletcher G M, Cardin A D
FEBS Lett. 1985 Oct 14;190(2):297-300. doi: 10.1016/0014-5793(85)81304-1.
Heparin was fractionated on an affinity column of bovine milk lipoprotein lipase (LpL) immobilized to Affi-Gel-15. The bound heparin, designated high-reactive heparin (HRH), enhanced LpL activity, presumably by stabilizing the enzyme against denaturation. The unbound heparin fraction had no observable effect on the initial rate of enzyme activity. However, at longer times of incubation there was inhibition of LpL activity. LpL-specific HRH also showed a high, Ca2+-dependent precipitating activity towards human plasma low density lipoproteins (LDL). Since LpL and LDL both bind to heparin-like molecules at the surface of the arterial wall, we suggest that their similar heparin-binding specificity may have physiological consequences as it relates to the development of atherosclerosis.
肝素在固定于Affi-Gel-15的牛乳脂蛋白脂肪酶（LpL）亲和柱上进行分级分离。结合的肝素，称为高反应性肝素（HRH），可能通过稳定酶使其不易变性来增强LpL活性。未结合的肝素部分对酶活性的初始速率没有可观察到的影响。然而，在较长的孵育时间下，LpL活性受到抑制。LpL特异性HRH对人血浆低密度脂蛋白（LDL）也表现出高的、Ca2+依赖性沉淀活性。由于LpL和LDL都能与动脉壁表面的类肝素分子结合，我们认为它们相似的肝素结合特异性可能对动脉粥样硬化的发展具有生理影响。
