通过羟基磷灰石高效液相色谱法分离冠状病毒包膜糖蛋白E2的亚基。
Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite high-performance liquid chromatography.
作者信息
Ricard C S, Sturman L S
出版信息
J Chromatogr. 1985 Jun 19;326:191-7. doi: 10.1016/s0021-9673(01)87445-8.
Abstract
The coronavirus glycoprotein E2, which is responsible for virus attachment to cell receptors and virus-induced cell fusion, was purified by solubilization of virions with Triton X-114 and phase fractionation. Native E2 and tryptic subunits of the glycoprotein were separated by size-exclusion high-performance liquid chromatography (HPLC). Two distinct 90 kD E2 subunits, which had identical electrophoretic mobilities when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were separated by hydroxyapatite HPLC in the presence of sodium dodecyl sulfate.
摘要
冠状病毒糖蛋白E2负责病毒与细胞受体的附着以及病毒诱导的细胞融合，通过用Triton X-114溶解病毒粒子并进行相分离来纯化。糖蛋白的天然E2和胰蛋白酶亚基通过尺寸排阻高效液相色谱（HPLC）分离。在十二烷基硫酸钠存在下，通过羟基磷灰石HPLC分离出两个不同的90 kD E2亚基，当通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析时，它们具有相同的电泳迁移率。
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