Primary structure of wheat germ agglutinin isolectin 2. Peptide order deduced from X-ray structure.
Primary structure of wheat germ agglutinin isolectin 2. Peptide order deduced from X-ray structure.
复制标题
小麦胚芽凝集素异凝集素 2 的一级结构。从 X 射线结构推导出的肽序。
DOI：
10.1021/bi00297a017
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发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Peterson,DL
中科院分区：
文献类型：
--
作者：
Wright,CS;Gavilanes,F;Peterson,DL
Christine Schubert Wright，Francisco Gavilanes，1和Darrell L.Peterson摘要：利用X射线结晶学中已知的三维结构，用顺序Edman降解法测定了小麦胚芽凝集素异凝素2的完整氨基酸序列。S-羧甲基化蛋白经热裂解，得到2~18个残基的多肽，经凝胶过滤和高效液相色谱分离纯化。肽序列的建立主要是通过将(羧甲基)半胱氨酸与X射线结构中明确定义的半胱氨酸位置相匹配，从而满足小麦胚凝集素的所有四个同构域(A、B、C和D)中观察到的二硫键重复模式，以及通过检查10个胰蛋白酶多肽的氨基酸组成和末端序列来建立的。多肽对这些区域的独特分配与所有不变量一致
Christine Schubert Wright,* Francisco Gavilanes, 1 and Darrell L. Peterson abstract: The complete amino acid sequence of wheat germ agglutinin isolectin 2 has been determined by the method of sequential Edman degradation and with the aid of the three-dimensional structure known from X-ray crystallography. Peptides ranging from 2 to 18 residuesin length were obtained by thermolysin digestion of the S-carboxymethylated protein and purified by gel filtration and high-performance liquid chromatography. The peptide order was established primarily by matching (carboxymethyl) cysteines with the clearly defined half-cystine positions in the X-ray structure, thereby satisfying the disulfide repeat pattern observed in all four isostructural domains (A, B, C, and D) of wheat germ agglutinin, and by examination of amino acid compositions and terminal se-quences of ten tryptic peptides. The unique assignment of peptides to these domains was consistent with all invariant