FOUGEREAU M, EDELMAN G M
J Exp Med. 1965 Mar 1;121(3):373-93. doi: 10.1084/jem.121.3.373.
The relationships between the polypeptide chains of gammaG immunoglobulin and fragments of the molecule produced by papain and pepsin have been investigated. Specific procedures were employed including peptide mapping of tryptic hydrolysates and analysis of molecules reconstituted from chains labeled with different iodine isotopes. By these means, the Fab fragment was shown unequivocally to consist of the light chain and a portion of the heavy chain, the Fd fragment. The Fc fragment was found to be comprised of the residual portions of the heavy chain. These findings support the gross arrangement of chains embodied in recent models of the gammaG immunoglobulin molecule. The present studies have also provided additional information on the susceptibility of gammaG immunoglobulin to proteolytic cleavage. It was found that the portion of heavy chains corresponding to the Fd fragment was extensively cleaved by papain.
已对γG免疫球蛋白的多肽链与木瓜蛋白酶和胃蛋白酶产生的分子片段之间的关系进行了研究。采用了特定的程序，包括胰蛋白酶水解产物的肽图谱分析以及对由用不同碘同位素标记的链重构的分子进行分析。通过这些方法，明确显示Fab片段由轻链和重链的一部分即Fd片段组成。发现Fc片段由重链的剩余部分组成。这些发现支持了γG免疫球蛋白分子近期模型中所体现的链的总体排列。本研究还提供了关于γG免疫球蛋白对蛋白水解切割敏感性的更多信息。发现与Fd片段相对应的重链部分被木瓜蛋白酶广泛切割。
