霍利斯弧菌和副溶血性弧菌产生的溶血素的氨基酸序列比较分析。
Comparative amino acid sequence analysis of hemolysins produced by Vibrio hollisae and Vibrio parahaemolyticus.
作者信息
Yoh M, Honda T, Miwatani T, Tsunasawa S, Sakiyama F
机构信息
Department of Bacteriology and Serology, Osaka University, Japan.
出版信息
J Bacteriol. 1989 Dec;171(12):6859-61. doi: 10.1128/jb.171.12.6859-6861.1989.
Abstract
Vibrio hollisae produces a hemolysin (Vh-rTDH) that is related to the thermostable direct hemolysin of Vibrio parahaemolyticus (Vp-TDH). Although both hemolysins are essentially similar biologically and immunologically, they differ markedly in heat stability; Vp-TDH is heat stable, whereas Vh-rTDH is heat labile. To elucidate the relationships between their characteristics and molecular structures, we analyzed the amino acid sequence of Vh-rTDH and compared it with that of Vp-TDH. Vh-rTDH consisted of 165 residues, of which 23 residues, spread over the peptide chain, differed from those of Vp-TDH.
摘要
霍利斯弧菌产生一种溶血素（Vh-rTDH），它与副溶血性弧菌的耐热直接溶血素（Vp-TDH）相关。尽管这两种溶血素在生物学和免疫学上基本相似，但它们在热稳定性上有显著差异；Vp-TDH是耐热的，而Vh-rTDH是热不稳定的。为了阐明它们的特性与分子结构之间的关系，我们分析了Vh-rTDH的氨基酸序列，并将其与Vp-TDH的氨基酸序列进行了比较。Vh-rTDH由165个残基组成，其中分布在肽链上的23个残基与Vp-TDH的残基不同。
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