EDP208接合菌毛的N端氨基酸测序
N-terminal amino acid sequencing of EDP208 conjugative pili.
作者信息
Frost L S, Armstrong G D, Finlay B B, Edwards B F, Paranchych W
出版信息
J Bacteriol. 1983 Feb;153(2):950-4. doi: 10.1128/jb.153.2.950-954.1983.
Abstract
EDP208 conjugative pili contain a single polypeptide subunit of 11,500 daltons with a blocked N-terminus. This N-terminal blocking moiety was identified as an N-acetyl group by 1H nuclear magnetic resonance analysis of an N-terminal tripeptide isolated from pronase digests of EDP208 pilin. Limited acid hydrolysis of the tripeptide allowed its sequence to be determined as acetyl-NH-Thr-Asp-Leu. Trypsin digestion of EDP208 pilin resulted in the quantitative release of a fragment containing 12 residues from the N-terminus of the protein. The sequence of this dodecapeptide was determined to be acetyl-NH-Thr-Asp-Leu-Leu-Ala-Gly-Gly-Lys-Asp-Val-Asp-Lys.
摘要
EDP208接合菌毛含有一个11500道尔顿的单一多肽亚基，其N端被封闭。通过对从EDP208菌毛蛋白的链霉蛋白酶消化物中分离出的N端三肽进行1H核磁共振分析，确定该N端封闭部分为N-乙酰基。对该三肽进行有限的酸水解，确定其序列为乙酰基-NH-苏氨酸-天冬氨酸-亮氨酸。用胰蛋白酶消化EDP208菌毛蛋白，导致从该蛋白质的N端定量释放出一个含有12个残基的片段。该十二肽的序列被确定为乙酰基-NH-苏氨酸-天冬氨酸-亮氨酸-亮氨酸-丙氨酸-甘氨酸-甘氨酸-赖氨酸-天冬氨酸-缬氨酸-天冬氨酸-赖氨酸。
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本文引用的文献
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J Bacteriol. 1983 Feb;153(2):955-61. doi: 10.1128/jb.153.2.955-961.1983.
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