Regulation of elastolysis of insoluble elastin by human leukocyte elastase: stimulation by lysine-rich ligands, anionic detergents, and ionic strength.
Regulation of elastolysis of insoluble elastin by human leukocyte elastase: stimulation by lysine-rich ligands, anionic detergents, and ionic strength.
复制标题
人白细胞弹性蛋白酶对不溶性弹性蛋白弹性分解的调节：富含赖氨酸的配体、阴离子去污剂和离子强度的刺激。
DOI：
10.1021/bi00284a027
复制
发表时间：
1983
期刊：
影响因子：
2.9
通讯作者：
Wohl,H
中科院分区：
文献类型：
--
作者：
Lonky,SA;Wohl,H
Stewart A.Lonky*和Herbert Wohl摘要：人白细胞弹性蛋白酶(HL Elastase)活性受到阳离子、莱辛里奇、肝素中和蛋白血小板因子4[PF4；Lonky，S.A.，&Wohl，H.(1981)J.Clin]的刺激。投资。67,817]。聚合物长度大于4的寡聚酶和富含赖氨酸的组蛋白也能刺激HL弹性蛋白酶。这种对HL弹性蛋白酶弹性分解活性的刺激依赖于聚合物的长度，并且当富含赖氨酸的配体被预吸附到不溶的弹性蛋白上时，这种刺激可以重复。虽然富含赖氨酸的配体的结合本质上是静电的，但在2.0M的氯化钠中，HL弹性蛋白酶与弹性蛋白的结合保持了接近90%的控制值。HL弹性蛋白酶与底物结合的静电性质体现在它与富含赖氨酸的配体的结合部位的竞争，以及对预涂有阴离子去污剂十二烷基硫酸钠的弹性蛋白的适度增强。尽管预涂有富含赖氨酸配体的弹性蛋白是HL弹性蛋白酶的较好底物，
Stewart A. Lonky* and Herbert Wohl abstract: Human leukocyte elastase (HL elastase) activity is stimulated against insoluble elastin by the cationic, lysinerich, heparin-neutralizing protein platelet factor 4 [PF4; Lonky, S. A., & Wohl, H.(1981) J. Clin. Invest. 67, 817]. Stimulation of HL elastase is also inducedby oligolysines of a polymer length greater than four and by lysine-rich histones. This stimulation of HL elastase elastolytic activity is dependent on polymer length and can be duplicated when lysine-rich ligands are preadsorbed onto the insoluble elastin. While the binding of lysine-richligands is electrostatic in nature, the binding ofHL elastase to elastin remains near 90% of control values in 2.0 M NaCl. The electrostatic nature of HL elastase binding to substrate is seen in its competition for binding sites with lysine-rich ligands and in the moderate enhancement of HL elastase activity against elastin precoated with the anionic detergent sodium dodecyl sulfate. Although elastin precoated with lysine-rich ligands is a better substrate for HL elastase,