Cebra J J, Givol D, Porter R R
Biochem J. 1968 Mar;107(1):69-77. doi: 10.1042/bj1070069.
Fragment C-1, the N-terminal half of the heavy chain of rabbit immunoglobulin G, was prepared by cyanogen bromide cleavage from the heavy chain of immunoglobulin G obtained both from the pooled serum of normal rabbits and from specific anti-dinitrophenyl antibody. Tryptic digestion of fragment C-1 after the lysine residues had been allowed to react with S-ethyl trifluorothioacetate led to the isolation of six peptides from inert immunoglobulin G and specific antibody that appear to account for most of this section of the heavy chain. This approach should make possible comparative sequence studies of the Fd section of the heavy chain from different allotypes and from specific antibodies.
片段C-1是兔免疫球蛋白G重链的N端半段,通过溴化氰裂解从正常兔混合血清和特异性抗二硝基苯基抗体中获得的免疫球蛋白G重链制备而成。在赖氨酸残基与S-乙基三氟硫代乙酸酯反应后,对片段C-1进行胰蛋白酶消化,从惰性免疫球蛋白G和特异性抗体中分离出六种肽,这些肽似乎构成了重链这一部分的大部分。这种方法应该能够对来自不同同种异型和特异性抗体的重链Fd段进行比较序列研究。