髓鞘膜碱性蛋白的氨基酸序列。
Amino acid sequence of the basic protein of the myelin membrane.
作者信息
Eylar E H
出版信息
Proc Natl Acad Sci U S A. 1970 Nov;67(3):1425-31. doi: 10.1073/pnas.67.3.1425.
Abstract
The amino acid sequences of the encephalitogenic basic protein, A1, from bovine and human myelin are similar, differing by only 11 residues. The sequence reveals that while basic residues are spread randomly over most of the polypeptide chain, several regions (8-10 residues) exist that are nonpolar in character. The bovine protein has 170 residues with molecular weight 18,400. The human protein, which has an additional His-Gly sequence, contains 172 residues. The major encephalitogenic determinant (tryptophan region) of the bovine protein differs from the human only by a lysine to arginine substitution. The structural features of the A1 protein are discussed, with special reference to its role in stabilization of the myelin membrane, and its relation to multiple sclerosis.
摘要
来自牛和人髓磷脂的致脑炎性碱性蛋白A1的氨基酸序列相似，仅相差11个残基。该序列显示，虽然碱性残基随机分布在多肽链的大部分区域，但存在几个（8 - 10个残基）具有非极性特征的区域。牛蛋白有170个残基，分子量为18,400。人蛋白含有172个残基，还有一个额外的His - Gly序列。牛蛋白的主要致脑炎性决定簇（色氨酸区域）与人类的仅在赖氨酸到精氨酸的替换上有所不同。本文讨论了A1蛋白的结构特征，特别提及了它在髓磷脂膜稳定中的作用及其与多发性硬化症的关系。
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