Givol D, Hurwitz E
Biochem J. 1969 Nov;115(3):371-5. doi: 10.1042/bj1150371.
Goat immunoglobulin G (IgG) was isolated and characterized. The molecular weights of the IgG and its heavy chains and light chains were found to be 144000, 53600 and 23000 respectively. The light chain corresponds to human L type as was shown by the absence of C-terminal S-carboxymethylcysteine and its high content of N-terminal pyrrolid-2-one-5-carboxylic acid (PCA). The major C-terminal residue of the light chain was serine and the major N-terminal dipeptide was PCA-Ala (0.6mole/mole). The major C-terminal residue of the heavy chain was glycine and the N-terminal sequence of the heavy chain is PCA-Val-Gln. This tripeptide was obtained in a 70% yield.
山羊免疫球蛋白G（IgG）被分离并进行了特性分析。发现IgG及其重链和轻链的分子量分别为144000、53600和23000。轻链对应于人L型，这是通过缺乏C末端S-羧甲基半胱氨酸及其高含量的N末端吡咯烷-2-酮-5-羧酸（PCA）所表明的。轻链的主要C末端残基是丝氨酸，主要的N末端二肽是PCA-Ala（0.6摩尔/摩尔）。重链的主要C末端残基是甘氨酸，重链的N末端序列是PCA-Val-Gln。该三肽的产率为70%。
