Egg white avidin. 3. Sequence of the 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit.
Egg white avidin. 3. Sequence of the 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit.
复制标题
蛋清亲和素。
DOI：
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发表时间：
1971
影响因子：
4.8
通讯作者：
T. S. Huang
中科院分区：
文献类型：
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作者：
R. Delange;T. S. Huang
通过对鸡卵白色亲和素蛋白中4个溴化氰肽和15个胰蛋白酶肽的序列分析，确定了该蛋白的氨基酸序列。抗生物素蛋白由四条基本相同的多肽链组成，每条多肽链含有128个氨基酸残基，在天冬酰胺残基17处连接有碳水化合物部分。每条链具有NH 2-末端丙氨酸、COOH-末端谷氨酸和残基4和83之间的链内二硫键，但大约一半的链在残基34处具有异亮氨酸，另一半在该位置处具有苏氨酸。溴化氰与抗生物素蛋白的反应代表了Met-Ser或Met-Thr键部分断裂的另一个例子，尽管甲硫氨酰残基定量转化为高丝氨酰残基。
Abstract The complete amino acid sequence of chicken egg white avidin has been elucidated from sequence studies on 4 cyanogen bromide peptides and 15 tryptic peptides obtained from the protein. Avidin consists of four essentially identical polypeptide chains, each containing 128 amino acid residues with a carbohydrate moiety attached at asparaginyl Residue 17. Each chain has NH2-terminal alanine, COOH-terminal glutamic acid, and an intrachain disulfide bond between Residues 4 and 83, but approximately half of the chains have isoleucine at Residue 34, and the other half have threonine at this position. No other evidence of heterogeneity in the sequence was found. The cyanogen bromide reaction with avidin represents another example of partial cleavage at Met-Ser or Met-Thr bonds, despite quantitative conversion of the methionyl residue to a homoseryl residue.