PURIFICATION AND PARTIAL CHARACTERIZATION OF A TYPE-SPECIFIC ANTIGEN OF RICKETTSIA-TSUTSUGAMUSHI
PURIFICATION AND PARTIAL CHARACTERIZATION OF A TYPE-SPECIFIC ANTIGEN OF RICKETTSIA-TSUTSUGAMUSHI
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DOI：
10.1128/iai.57.5.1427-1431.1989
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发表时间：
1989-05-01
影响因子：
3.1
通讯作者：
HAYASHI, K
中科院分区：
文献类型：
--
作者：
OHASHI, N;TAMURA, A;HAYASHI, K
通过温和的阴离子去污剂处理、凝胶过滤和反相高效液相色谱的组合，从三种原型菌株（Gilliam、Karp和Kato）中纯化出恙虫病立克次体包膜中的型特异性抗原（54- 56千道尔顿多肽）。从三个菌株纯化的抗原显示具有相似的氨基酸组成：主要是天冬氨酸，谷氨酸和甘氨酸，与较少量的半胱氨酸，甲硫氨酸和酪氨酸。三株病毒N端氨基酸序列同源性为74.3%。
A type-specific antigen (54- to 56-kilodalton polypeptide) in the envelope of Rickettsia tsutsugamushi was purified from each of three prototype strains (Gilliam, Karp, and Kato) by a combination of mild anionic detergent treatment, gel filtration, and reverse-phase high-performance liquid chromatography. The purified antigens from the three strains were shown to have similar amino acid compositions: primarily aspartic acid, glutamic acid, and glycine, with lesser amounts of cysteine, methionine, and tyrosine. The N-terminal amino acid sequences of the antigens were 74.3% homologous among the three strains.