Mole L E, Jackson S A, Porter R R, Wilkinson J M
Biochem J. 1971 Sep;124(2):301-18. doi: 10.1042/bj1240301.
The sequence has been completed of the N-terminal 94 residues of the variable section of the Fd fragment of heavy chains from rabbit immunoglobulin G (IgG) of allotype As1. Most of the sequence of the same section from IgG of allotype Aa3 is also reported. These results, in conjunction with a substantial sequence of the variable region of allotype Aa2 reported elsewhere (Fleischman, 1971), show the presence of 16 positions (including six consecutive positions) in which the residue present correlates with the allotype. No allotype-related sequence variation has been found in the constant section of the Fd fragment. This evidence supports the view that two genes code for the heavy chain and it can be used as evidence in favour of somatic mutation as the origin of the variability in the sequence of the N-terminal section. The evolutionary origin of the ;a' locus allotypes of rabbit immunoglobulins remains obscure.
已完成对同种异型As1的兔免疫球蛋白G（IgG）重链Fd片段可变区N端94个残基的测序。还报道了同种异型Aa3的IgG相同区段的大部分序列。这些结果，连同其他地方报道的同种异型Aa2可变区的大量序列（弗莱施曼，1971年），表明存在16个位置（包括六个连续位置），其中存在的残基与同种异型相关。在Fd片段的恒定区未发现与同种异型相关的序列变异。这一证据支持了两个基因编码重链的观点，并且可以用作支持体细胞突变是N端区段序列变异性起源的证据。兔免疫球蛋白“a”位点同种异型的进化起源仍然不明。
