Turner M W, Bennich H
Biochem J. 1968 Mar;107(2):171-8. doi: 10.1042/bj1070171.
A fragment termed fragment Fc' and a related fragment termed fragment pFc' produced by the actions of papain and pepsin respectively on human immunoglobulin G have been isolated and characterized. Amino acid analyses and experiments utilizing cyanogen bromide to cleave the methionyl bonds of the Fc' and pFc' fragments make it possible to locate both fragments within the known chain structure of the immunoglobulin G molecule. The pFc' fragment is probably a non-covalently linked dimer situated at the C-terminal end of the molecule, containing about 232 amino acid residues and having a molecular weight of 26000. The Fc' fragment is a similar dimer of about 182 residues extending from near residue 14 to near residue 105 (numbered from the C-terminal end) of the gamma-chain and has a molecular weight of 21000.
分别由木瓜蛋白酶和胃蛋白酶作用于人类免疫球蛋白G产生的一个称为Fc'片段和一个相关的称为pFc'片段已被分离和鉴定。氨基酸分析以及利用溴化氰裂解Fc'和pFc'片段中甲硫氨酰键的实验使得在免疫球蛋白G分子已知的链结构中定位这两个片段成为可能。pFc'片段可能是位于分子C末端的非共价连接二聚体，含有约232个氨基酸残基，分子量为26000。Fc'片段是一个类似的二聚体，约有182个残基，从γ链的近14位残基延伸至近105位残基（从C末端编号），分子量为21000。
