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From the Laboratory of Protein Chemistry, Institut de Recherches Scientifiques sur le Cancer, C.N.R.S., 94800 Villejuif, France
Abstract
Rabbit antibodies prepared against two purified 7S BALB/c myeloma proteins, A2 (
1,
) and MOPC 195 (
2b,
), and solid-phase absorbed so as to contain only anti-heavy (H) chain specificities bound to 32 to 35% of C57BL/6 lymph node lymphocytes (about 80% of the B lymphocytes). A similar staining frequency was obtained with solid-phase absorbed antibodies to the Fab fragment and the heavy chain of the A2 protein. On the other hand, antibodies to other 7S proteins (MOPC 21 (
1,
), J606 (
3,
), and MOPC 173 (
2a,
)), as well as anti-Fc
1, anti-Fc
2a and anti-idiotypic antibodies either failed to bind to the cells, or bound to a small percentage of these. Employing a method of quantitative inhibition of cell-surface-binding capacity, it was found that the surface binding of the anti-A2 and anti-MOPC 195 antibodies was strongly inhibited by the MOPC 104E (µ,
1) and J558 (
,
1) proteins. There was also a reciprocal inhibition by the A2 and MOPC 195 proteins. Purified normal serum IgG1 and IgG2a were also strongly inhibitory. However, eight other BALB/c myeloma proteins of various classes were weakly, or noninhibitory. Only the homologous A2 Fab fragment, and H and light (L) chains inhibited the anti-A2 antibodies. The homologous and heterologous Fc fragments were not inhibitory. These results, added to the selective inhibitory behavior of the myeloma proteins, which is unrelated to either their H or L chain isotypic designation, suggest that the antigens involved are localized in H chain the variable region. The findings implicate that the bulk of C57BL/6 lymph node B lymphocytes expresses a surface H chain variable region subgroup antigen that corss-reacts with the A2, MOPC 195, MOPC 104E, and J558 myeloma proteins.
Footnotes
1 This work was supported in part in part by a Délégation pour la Recherche Scientifique et Technique Grant 6501600.
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