A2m(2)同种异型的人IgA2免疫球蛋白α2重链的完整氨基酸序列。
Complete amino acid sequence of the alpha 2 heavy chain of a human IgA2 immunoglobulin of the A2m (2) allotype.
作者信息
Toraño A, Putnam F W
出版信息
Proc Natl Acad Sci U S A. 1978 Feb;75(2):966-9. doi: 10.1073/pnas.75.2.966.
Abstract
The complete amino acid sequence of the alpha 2 heavy chain of a human IgA2 immunoglobulin of the A2m(2) allotype has been determined and is compared to the sequence of the alpha 1 chain of the human IgA1 subclass. The characteristic differences between the alpha 1 and alpha 2 chains are greatest in the hinge region and in the location and number of the oligosaccharides. Apart from the duplication in the hinge region of alpha 1 and the deletion in alpha 2, there are 23 amino acid exchanges in the constant (C) regions of the two chains. Accepted mutations are related to the surface accessibility of the residues and the proximity of carbohydrate. The results indicate that human IgA and IgG subclasses arose late in evolution and reflect similar mutationa pressures.
摘要
已确定人A2m(2)同种异型IgA2免疫球蛋白α2重链的完整氨基酸序列，并将其与人类IgA1亚类α1链的序列进行比较。α1链和α2链之间的特征性差异在铰链区以及寡糖的位置和数量上最为显著。除了α1铰链区的重复和α2的缺失外，两条链的恒定（C）区还有23个氨基酸交换。公认的突变与残基的表面可及性和碳水化合物的接近程度有关。结果表明，人类IgA和IgG亚类在进化后期出现，并反映了相似的突变压力。
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