(抗体结构的规则。的主要结构单克隆IgG1免疫球蛋白(Nie骨髓瘤蛋白质)。三世。H-chain的糜蛋白酶的肽,对齐的胰蛋白酶的肽和讨论完成结构)。
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Ponstingl H, Hilschmann N
(抗体结构的规则。的主要结构单克隆IgG1免疫球蛋白(Nie骨髓瘤蛋白质)。三世。H-chain的糜蛋白酶的肽,对齐的胰蛋白酶的肽和讨论完成结构)。
霍普Seylers Z杂志化学。1976年11月,357 (11):1571 - 604。
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826475年(在PubMed]
- 文摘
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在这个期末论文的完成主要结构H-chain免疫球蛋白的聂(IgG1 Gm1 + 17 +)建立了重叠的胰蛋白酶和糜蛋白酶的肽片段。前面的论文蛋白质的纯化处理,轻、重链的特征,溴化氰乳沟的纯化和表征产品,二硫键的位置,胰蛋白酶的肽的分离及其序列测定。Nie gamma1-chain由448个氨基酸残基。当蛋白质与其他H-chains相比,开关变量的常数部分发生在119/120的位置。基于氨基酸序列的变量部分蛋白质聂H-chains属于第三子群。它是第一个蛋白质测序的子群。与此同时其他几个已知蛋白质已被分配给相同的子群链氨基酸的基础上交流相比其他子组的成员。这证实了抗体进化起源的变异性,因此固定抗体的特定基因。此外蛋白质聂是第一个完全确定链与遗传因素Gm1 + 17 +。这些因素是共显性的遗传和本地化的常数gamma1-chain的一部分。 By comparison with protein Eu, which is Gml-, 4+ and therefore an allele of Nie, these serologically defined factors are correlated with Eu. Besides the amino acid exchanges caused by the Gm-factors we elucidated a series of differences to the constant part of the protein Eu. These differences include 6 amide postions and the sequence from residues 387 to 391. Using the structure of IgG1 Nie as an example some rules for the evolution of immunoglobulin sequences have been described. In particular the "elongation-rule" and the "Disulfide-rule" are discussed. While chain-elongation of the H-chains can simply be explained by repeated gene duplications of a basic unit containing ca 110 amino acids, the location of disulfide bonds is determined partly by gene duplication, which implies multiplication of evolutionary "old" cystein residues and partly by the relatively recent acquisition of "new" cystein in appropriate sites. Most evident is the origin of the "hindge-region" by partial gene duplication on the C-terminal residues of the first homology region.