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结节拟杆菌216株菌毛蛋白的一级结构:与198株相应蛋白的比较

Primary structure of pilin protein from Bacteroides nodosus strain 216: comparison with the corresponding protein from strain 198.

作者信息

McKern N M, O'Donnell I J, Stewart D J, Clark B L

出版信息

J Gen Microbiol. 1985 Jan;131(1):1-6. doi: 10.1099/00221287-131-1-1.

Abstract

The amino acid sequence of pilin protein from Bacteroides nodosus strain 216 was determined. The protein had a calculated molecular weight of 15962 and contained the same number of amino acid residues (151) as the pilin from the previously sequenced strain 198. The sequence of the first 44 residues was common to both strains, including the unusual amino-terminal amino acid, N-methylphenylalanine. Of the remaining 107 residues, 37% of them differed between the two strains. Comparison of hydrophilicity profiles constructed from the sequence data indicated that a conserved region around residues 71-72 was probably the site of an antigenic determinant.

摘要

已确定结节拟杆菌216菌株菌毛蛋白的氨基酸序列。该蛋白的计算分子量为15962,所含氨基酸残基数量(151个)与之前测序的198菌株的菌毛蛋白相同。两菌株前44个残基的序列相同,包括不寻常的氨基末端氨基酸N - 甲基苯丙氨酸。在其余107个残基中,两菌株间有37%不同。根据序列数据构建的亲水性图谱比较表明,71 - 72位残基周围的保守区域可能是抗原决定簇的位点。

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