Conde F P, Deverson E V, Milstein C P
Eur J Immunol. 1975 Apr;5(4):291-3. doi: 10.1002/eji.1830050416.
Sheep immunoglobulin IgG1 and immunoglobulin IgG2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and purified, and the amino acid sequences gamma1 and gamma2 heavy chains had the identical sequence: Met-His-Glx-Ala-Leu-His-Asx-His-Tyr-Thr-Glx-Lys-Ser-Ile-Ser-Lys-Pro-Pro-Gly. Comparison with the C-terminal peptides of other species, reported in the literature, suggests that the subclasses are the results of recent evolutionary processes. Residues at position 4 from the C-terminus may be phylogenetically related.
绵羊免疫球蛋白IgG1和免疫球蛋白IgG2重链用溴化氰处理。从重链C末端分离并纯化各组分,γ1和γ2重链的氨基酸序列相同:甲硫氨酸-组氨酸-谷氨酰胺-丙氨酸-亮氨酸-组氨酸-天冬酰胺-组氨酸-酪氨酸-苏氨酸-谷氨酰胺-赖氨酸-丝氨酸-异亮氨酸-丝氨酸-赖氨酸-脯氨酸-脯氨酸-甘氨酸。与文献报道的其他物种的C末端肽段进行比较表明,这些亚类是近期进化过程的结果。C末端第4位的残基可能与系统发育有关。