Fab-related fragments of human IgG produced by partial tryptic proteolysis

G. A. Medgyesi, Mária Csécsi-Nagy, G. Gorini, Éva Puskás, J. Gergely, M. Sajgó, A. Czuppon

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A 2·2-2·5 S, Fab-related fragment (tFab′) was isolated from trypic digests of normal human IgG and of IgG1 myeloma proteins. Reductive cleavage of this gragment led to dissociation into polypeptide constituents of a mol. wt corresponding to one half of a light chain or of an Fd piece. Indirect evidence is presented that the disulphide bridge linking a κ to a γ 1 heavy chain is contained by tFab′. Heterologous anti-Fab immune sera precipitated fragment tFab′ as well as Fab (produced by papain) or the 3·9-4·4 S tryptic Fab fragment (tFab). Fragment tFab′ from a myeloma protein was found to be deficient in individual specific antigenic determinants of the parent protein. 'Trypsin-site' (determinant of IgG revealed by tryptic proteolysis) was found to be fully retained by tFab′, while the Gm(f) allotype-determinant was not detectable on it serologically.

Original languageEnglish
Pages (from-to)509-515
Number of pages7
Issue number8
Publication statusPublished - Aug 1973


ASJC Scopus subject areas

  • Medicine(all)

Cite this

Medgyesi, G. A., Csécsi-Nagy, M., Gorini, G., Puskás, É., Gergely, J., Sajgó, M., & Czuppon, A. (1973). Fab-related fragments of human IgG produced by partial tryptic proteolysis. Immunochemistry, 10(8), 509-515. https://doi.org/10.1016/0019-2791(73)90222-X