Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B.
Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B.
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硫氧还蛋白。
DOI：
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发表时间：
1968
期刊：
影响因子：
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通讯作者：
A. Holmgren
中科院分区：
文献类型：
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作者：
A. Holmgren
肽A是硫氧还蛋白的C-末端溴化氰片段，用胰凝乳蛋白酶和胃蛋白酶降解。测定了12种胰凝乳蛋白酶肽和6种消化肽的部分序列以及三氟乙酰化肽A的N端胰蛋白酶肽。结果用于建立先前描述的肽A的胰蛋白酶肽的顺序，并导致肽A的完整氨基酸序列。
以前的实验已经确定了肽B的氨基酸序列，肽B是硫氧还蛋白的N-末端溴化氰片段，因此本实验结果给出了大肠杆菌B硫氧还蛋白的完整氨基酸序列。该分子在单个多肽链中含有108个残基，根据序列计算分子量为11，657。蛋白质的官能团位于32至35位，由两个半胱氨酸残基形成的二硫桥组成，两个半胱氨酸残基被甘氨酸和脯氨酸残基分开。未发现金属作为官能团的一部分。
Peptide A, the C-terminal cyanogen bromide fragment of thioredoxin, was degraded with chymotrypsin and pepsin. Partial sequences of 12 chymotryptic and 6 peptic peptides and the N-terminal tryptic peptide of trifluoro-acetylated peptide A were determined. The results were used to establish the order of the previously described tryptic peptides of peptide A and lead to the complete amino acid sequence of peptide A.
Previous experiments had established the amino acid sequence of peptide B, the N-terminal cyanogen bromide fragment of thioredoxin and the present results thus give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half-cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group.