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在Triton X-100存在的情况下,通过阴离子交换高效液相色谱法分离仙台病毒F蛋白。

Isolation of Sendai virus F protein by anion-exchange high-performance liquid chromatography in the presence of Triton X-100.

作者信息

Welling G W, Groen G, Welling-Wester S

出版信息

J Chromatogr. 1983 Aug 26;266:629-32. doi: 10.1016/s0021-9673(01)90932-x.

Abstract

Purified Sendai virions were treated with Triton X-100. The detergent extract containing the fusion protein (F) and the haemagglutinin-neuraminidase protein (HN) was subjected to anion-exchange high-performance liquid chromatography on a Mono Q (Pharmacia) column with 0.1% Triton X-100 in phosphate-buffered saline. HN was not retained by the column while elution with a salt gradient resulted in several peaks containing mainly or only F protein.

摘要

纯化的仙台病毒粒子用Triton X-100处理。含有融合蛋白(F)和血凝素神经氨酸酶蛋白(HN)的去污剂提取物在含有0.1% Triton X-100的磷酸盐缓冲盐水中,通过Mono Q(Pharmacia)柱进行阴离子交换高效液相色谱分析。HN不被柱子保留,而用盐梯度洗脱则产生几个主要或仅含F蛋白的峰。

相似文献

7
Purification strategies for Sendai virus membrane proteins.仙台病毒膜蛋白的纯化策略。
J Chromatogr. 1987 Jun 26;397:165-74. doi: 10.1016/s0021-9673(01)84999-2.

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