Premium
Studies on Fd Fragments of Human Immunoglobulins
Author(s) -
ZEGERS B. J. M.,
BALLIEUX R. E.,
LOGHEM E.
Publication year - 1975
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1975.tb02613.x
Subject(s) - antiserum , antibody , myeloma protein , immunoglobulin light chain , cyanogen bromide , antigen , chemistry , microbiology and biotechnology , multiple myeloma , biology , immunology , peptide sequence , biochemistry , gene
Earlier studies on antisera against Fab of pooled human IgG and IgA myeloma proteins disclosed the presence of class‐specific Fd antibodies, the demonstration of which required interaction of heavy and light chains. To extend our knowledge about the antigenic structure of the Fd fragment of human immunoglobulins, antisera were prepared in rabbits against γ chains of pooled IgG and of four IgG1 myeloma proteins, an Fdγ fragment and a cyanogen bromide‐produced CH1 preparation of an IgG1 myeloma protein, and an Fd α fragment of an IgA1 myeloma protein. No antigenic determinants exclusively confined to the CH1 region of intact human IgG could be demonstrated with these antisera. The antigenic structure of CH1 in intact immunoglobulins may thus only be defined by light‐chain‐dependent determinants.