The complete amino acid sequence of a prototype immunoglobulin-lambda light-chain-type amyloid-fibril protein AR.
The complete amino acid sequence of a prototype immunoglobulin-lambda light-chain-type amyloid-fibril protein AR.
复制标题
原型免疫球蛋白-lambda 轻链型淀粉样原纤维蛋白 AR 的完整氨基酸序列。
作者：
K. Sletten;J. Natvig;G. Husby;J. Juul
阐明了免疫球蛋白轻链型（AL）淀粉样纤维蛋白的氨基酸序列。序列测定包括用胰蛋白酶、嗜热菌蛋白酶和胃蛋白酶消化蛋白质。发现该蛋白质由154个氨基酸残基组成，因此缺少轻链恒定区的约一半。在C-末端区域观察到多肽长度的一定异质性。CDR（互补决定区）1和FR（框架区）3的氨基酸序列表明该蛋白的寡克隆起源。通过将蛋白AR的一级结构与其它λ-链甚至κ-链进行比较，揭示了蛋白AR具有两个天冬氨酸残基的插入，即残基68和69，这在轻链中以前没有报道过。可变区中的整体序列同源性表明，蛋白质AR与V λ V比与其他亚组更相似[Kabat，Wu & Bilofsky（1979）Variable regions of Immunoglobulin Chains，Medical Computer Systems，Bolt，Beranek and纽曼，剑桥，MA]。
The amino acid sequence of an amyloid-fibril protein of immunoglobulin light-chain type (AL) was elucidated. The sequence determination involved digesting the protein with trypsin, thermolysin and pepsin. The protein was found to consist of 154 amino acid residues and is thus missing about half of the constant region of a light chain. A certain heterogeneity in the length of the polypeptide was observed in the C-terminal region. The amino acid sequence from CDR (complementary-determining region) 1 and FR (framework region) 3 indicated an oligoclonal origin of the protein. By comparing the primary structure of protein AR with other lambda- and even kappa-chains, it was revealed that protein AR had an insertion of two residues of aspartic acid, namely residues 68 and 69, which has not been reported previously in light chains. The overall sequence homology in the variable region showed that protein AR is more similar to V lambda V than to the other subgroups [Kabat, Wu & Bilofsky (1979) Variable regions of Immunoglobulin Chains, Medical Computer Systems, Bolt, Beranek and Newman, Cambridge, MA].