| Literature DB >> 4541124 |
V A Bokisch, J W Chiao, D Bernstein.
Abstract
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.Entities:
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Year: 1973 PMID： 4541124 PMCID： PMC2139354 DOI： 10.1084/jem.137.6.1354
Source DB: PubMed Journal: J Exp Med ISSN： 0022-1007 Impact factor: 14.307