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QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES
In guinea pig purified antihapten antibodies, the proportion of molecules bearing the κ- or λ-type of L chains (K or L molecules) may diverge markedly from that found in normal γ(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-λ-ch...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1966
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138265/ https://www.ncbi.nlm.nih.gov/pubmed/4162733 |
Sumario: | In guinea pig purified antihapten antibodies, the proportion of molecules bearing the κ- or λ-type of L chains (K or L molecules) may diverge markedly from that found in normal γ(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-λ-chain antiserum. Anti-DNP antibodies isolated 3 wk after immunization of guinea pigs with DNP(65)-BGG antibodies, contain less than 1% of L molecules, while in pipsyl antibodies, isolated from the sera of animals immunized with pipsyl-BGG, the proportion of L molecules is significantly greater than in normal γ(2)-globulins. Anti-DNP antibodies produced against conjugates of this hapten with carriers other than BGG (BSA, OVA, or poly-L-lysine) or with BGG with a small number of DNP groups (DNP(10)-BGG) contained a greater proportion of λ-chain bearing molecules than anti-DNP antibodies isolated from late sera of guinea pigs immunized with highly conjugated DNP(65)-BGG. An increased percentage of L molecules was detected in preparations of anti-DNP(65)-BGG antibodies isolated early (10 days), when compared to those isolated later during the course of immunization. However, the level of L molecules in all these anti-DNP antibody preparations was always considerably below that present in normal γ(2)-globulin. The relative amounts of L molecules in distinct immunoglobulin families (γ(1) and γ(2)) in antibody preparations isolated from individual animals was remarkably similar. |
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