ANALYSIS, PURIFICATION AND PROPERTIES OF A 50000-DALTON MEMBRANE-ASSOCIATED PHOSPHOPROTEIN FROM HUMAN PLATELETS
ANALYSIS, PURIFICATION AND PROPERTIES OF A 50000-DALTON MEMBRANE-ASSOCIATED PHOSPHOPROTEIN FROM HUMAN PLATELETS
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DOI：
10.1016/0021-9673(90)85057-3
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发表时间：
1990-11-23
期刊：
影响因子：
--
通讯作者：
WALTER, U
中科院分区：
文献类型：
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作者：
HALBRUGGE, M;WALTER, U
近年来，报道了抗人血小板46 000/50 000-道尔顿膜蛋白的单特异性抗血清的开发，该膜蛋白在完整的人血小板中响应于血管扩张剂而化学计量地可逆地磷酸化。使用这种抗血清，亚细胞分布和纯化的血管扩张刺激磷蛋白（VASP）从人血小板现在已经分析。人血小板的VASP主要是一种膜相关蛋白，可以通过盐提取和连续离子交换和染料配体色谱法纯化至表观均一性，纯化因子为1200，产率为13%。在还原和非还原条件下的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳表明，纯化的单体的VASP连接的链间二硫键。
Recently, the development of a monospecific antiserum against a 46 000/50 000-dalton membrane protein from human platelets which was stoichiometrically and reversibly phosphorylated in intact human platelets in response to vasodilators was reported. Using this antiserum, the subcellular distribution and the purification of this vasodilator-stimulated phosphoprotein (VASP) from human platelets has now been analysed. The VASP of human platelets is primarily a membrane-associated protein and can be purified to apparent homogeneity by salt extraction and sequential ion-exchange and dye-ligand chromatography with a purification factor of 1200 and a yield of 13%. Sodium dodecyl sulphate—polyacrylamide gel electrophoresis under reducing and non-reducing conditions indicated that purified monomers of this VASP are linked by interchain disulphide bonding.