Amino acid sequence of thermostable direct hemolysin produced by Vibrio parahaemolyticus.
Amino acid sequence of thermostable direct hemolysin produced by Vibrio parahaemolyticus.
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DOI：
10.1093/oxfordjournals.jbchem.a121882
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发表时间：
1987
影响因子：
2.7
通讯作者：
S. Tsunasawa;A. Sugihara;T. Masaki;F. Sakiyama;Y. Takeda;T. Miwatani;K. Narita
中科院分区：
文献类型：
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作者：
S. Tsunasawa;A. Sugihara;T. Masaki;F. Sakiyama;Y. Takeda;T. Miwatani;K. Narita
通过对BrCN肽、胰蛋白酶肽和无色杆菌蛋白酶I消化获得的重叠肽进行测序，确定了热稳定直接溶血素亚基的完整氨基酸序列，该亚基是由分离自副溶血弧菌的相同亚基组成的二聚体蛋白。该亚基由165个氨基酸残基组成，唯一的二硫键位于Cys 151和Cys 161之间。推测具有生物活性的溶血素是由非二硫键连接的亚基非共价结合而成。在本研究中阐明的溶血素的一级结构基本上是相同的，推导出的编码蛋白质的基因的核苷酸序列，但不同的9个氨基酸残基，这表明可能存在的多个基因的耐热直接溶血在副溶血弧菌。
The complete amino acid sequence of the subunit of thermostable direct hemolysin, a dimeric protein composed of identical subunits isolated from Vibrio parahaemolyticus, was determined by sequencing BrCN-peptides, their tryptic peptides, and overlaps obtained by Achromobacter protease I digestion. The subunit consists of 165 amino acid residues with the sole disulfide bond between Cys 151 and Cys 161. It is deduced that the biologically active hemolysin is formed by noncovalent association of subunits which are not linked together by disulfide bonds. The primary structure of hemolysin elucidated in the present study is essentially the same as that deduced from the nucleotide sequence of a gene encoding the protein but differs in 9 amino acid residues, suggesting the possibility of the presence of multiple genes for the thermostable direct hemolysin in Vibrio parahaemolyticus.