Premium
THE RETENTION OF 125 I‐IMMUNOGLOBULINS, IgG SUBUNITS AND ANTIGEN‐ANTIBODY COMPLEXES IN RAT FOOTPADS AND DRAINING LYMPH NODES
Author(s) -
Herd Zana L,
Ada GL
Publication year - 1969
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1969.5
Subject(s) - antibody , lymph , chemistry , albumin , human serum albumin , immunoglobulin g , bovine serum albumin , serum albumin , microbiology and biotechnology , immunoglobulin light chain , biochemistry , immunology , biology , pathology , medicine
Summary. Studies on the retention of 125 I‐labelled rat and rabbit immunoglobulins and subunits thereof in rat popliteal nodes indicate that the Fc fragment of IgG is important for maintaining a relatively high concentration of this immunoglobulin in lymph nodes. After footpad injections of the immunoglobulins and subunits, an approximate correlation was found between the initial rate of disappearance from the feet and the molecular size of the substances injected. This suggested that a major factor involved in removal of substances from rat footpads is their rate of diffusion. No correlation with molecular weight was fotind in the retention pattern of immunoglobulin subunits in the popliteal nodes which drained the footpads. Rabbit Fc fragment was retained 50 times better than rabbit Fab fragment in rat nodes 3 days after injection. Rabbit H chains were retained better than rabbit L chains. A peptide from the Fc region of rabbit heavy chains, C3, showed high retention in rat nodes and was retained better than IgG but not as well as Fc. Rat IgG and IgM were both retained better than rat Fab in rets. Human serum albumin complexes with rabbit anti‐human serum albumin IgG was retained at least 10 times better by rat nodes than human serum albumin alone. Human serum albumin bound to rabbit anti‐human serum albumin Fab was retained only about twice as well as human serum albumin alone.