Wolfenstein-Todel C, Frangione B, Franklin E C
Biochim Biophys Acta. 1975 Feb 27;379(2):627-37. doi: 10.1016/0005-2795(75)90169-5.
The amino acid sequence of the heavy chain of an IgA2, AIm(1) polymeric myeloma protein (Avil) was studied. Altogether, sequence data were obtained for some 130 residues. Including the amino acids placed by homology with IgA1, this accounts for some 170 residues, thus representing more than one-third of the alpha2 chain. The sequence includes 26 amino acids from the amino-terminal end (V-H III), and 25 residues at the "hinge" region. Of a total of 17 cysteine residues, 14 were located in regions of the molecule which were identical or homologous in the alpha1 and alpha2 chains. These striking homologies, together with the results obtained by diagonal maps of classes of IgA. Study of the cysteine-containing peptides of the J chain are consistent with the conclusion that the J chains associated with different classes of immunoglobulins are identical.
对一种IgA2、AIm(1)聚合性骨髓瘤蛋白(阿维尔)重链的氨基酸序列进行了研究。总共获得了约130个残基的序列数据。包括通过与IgA1同源性定位的氨基酸,这占了约170个残基,因此代表了α2链的三分之一以上。该序列包括来自氨基末端(V-H III)的26个氨基酸,以及“铰链”区的25个残基。在总共17个半胱氨酸残基中,14个位于α1和α2链中相同或同源的分子区域。这些显著的同源性,以及通过IgA类对角线图谱获得的结果。对J链含半胱氨酸肽段的研究与以下结论一致:与不同类免疫球蛋白相关的J链是相同的。