Purification and amino-terminal protein sequence analysis of the mumps virus fusion protein.
Purification and amino-terminal protein sequence analysis of the mumps virus fusion protein.
复制标题
腮腺炎病毒融合蛋白的纯化及氨基端蛋白序列分析。
DOI：
10.1016/0042-6822(85)90279-x
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发表时间：
1985
期刊：
影响因子：
3.7
通讯作者：
Goodman,HM
中科院分区：
文献类型：
--
作者：
Server,AC;Smith,JA;Waxham,MN;Wolinsky,JS;Goodman,HM
The fusion (F) protein of mumps virus was purified by immunoaffinity chromatography using an anti-F monoclonal antibody. The F protein was reduced and alkylated, and the F1and F2chains were isolated by high-pressure size exclusion chromatography. Twenty-three amino acid residues from the amino terminus of each chain were identified following automated Edman degradation. The amino-terminal sequence of the F1chain was homologous to previously reported F1sequences from three other paramyxoviruses (simian virus 5, Newcastle disease virus, and Sendai virus). Secondary structure predictions suggest an a-helical conformation for the mumps virus F1amino-terminal sequence. A helical wheel model of the paramyxovirus F1NH2terminus is presented which defines conserved and variable arcs of the helix and provides a spatial representation of this critical functional domain of the paramyxovirus fusion protein.
