The Journal of Experimental Medicine, Vol 137, 1354-1368,
Copyright © 1973 by The Rockefeller University Press
ISOLATION AND IMMUNOCHEMICAL CHARACTERIZATION OF RABBIT 7S ANTI-IGG WITH RESTRICTED HETEROGENEITY
Viktor A. Bokisch 1,
Jen Wei Chiao 1, and
David Bernstein 1
1 From The Rockefeller University, New York 10021
7S anti-IgGs were isolated from four rabbit antistreptococcal antisera by the use of immunoabsorbent columns. The isolated proteins were of restricted molecular heterogeneity; they formed a monodisperse band on microzone electrophoresis and had a limited number of light chain bands when analyzed on urea polyacrylamide gel. The binding site of the 7S anti-IgGs was detected in the F(ab')2 portion of the molecule. The binding site has antibody specificity for the Fc portion of IgG. For one 7S anti-IgG the combining site on the Fc portion could further be defined. A pepsin fragment of Fc, described as Pep-III', was a potent inhibitor of the coprecipitation of 7S anti-IgG with antigen-antibody complexes.
An idiotypic cross-reaction was detected between the 7S and 19S anti-IgGs isolated from the same rabbit with anti-idiotype sera prepared in guinea pigs. This idiotypic specificity was not detected in the 7S anti-IgGs of 20 other rabbits.
Submitted on January 22, 1973