Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1967 Oct 1;126(4):727–743. doi: 10.1084/jem.126.4.727

ANTIHAPTEN ANTIBODY SPECIFICITY AND L CHAIN TYPE

Victor Nussenzweig 1, Baruj Benacerraf 1
PMCID: PMC2138385  PMID: 4168100

Abstract

Two types of light polypeptide chain (κ and λ) are present in guinea pig immunoglobulins. The ratios of K/L molecules in anti-hapten antibodies differ sometimes markedly from that found in normal serum. Anti-DNP antibodies and anti-pipsyl antibodies have, respectively, a higher and a lower than normal K/L ratio. The possibility that the L chain type affects the range of configurations which the antibody-combining site may assume was investigated. Fractional precipitation of anti-DNP antibodies from serum of guinea pigs immunized with DNP44-BSA was performed using limiting amounts of antigen. Antibody fractions were purified from each precipitate, their affinities for ε-DNP-L-lysine measured by fluorescence quenching (K 0) and the K/L ratio estimated by precipitation with specific antisera. Increasing concentrations of L molecules were found in fractions with decreasing K 0. In other experiments, fractional precipitation and purification of antibodies which cross-react with DNP was performed in serum of animals immunized with pipsyl-BGG. The K/L ratio in antibodies isolated from these fractions was much higher than in fractions which do not cross-react with DNP. These results show that K molecules are better adapted to react with the DNP hapten than L molecules. The K/L ratio in anti-DNP antibody was shown to increase in the course of immunization, at the same time that the K 0 is increasing. This rise in K 0 is markedly delayed when larger doses of antigen are employed.

Full Text

The Full Text of this article is available as a PDF (943.2 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. EDELMAN G. M., BENACERRAF B., OVARY Z., POULIK M. D. Structural differences among antibodies of different specificities. Proc Natl Acad Sci U S A. 1961 Nov 15;47:1751–1758. doi: 10.1073/pnas.47.11.1751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. EDELMAN G. M., OLINS D. E., GALLY J. A., ZINDER N. D. RECONSTITUTION OF IMMUNOLOGIC ACTIVITY BY INTERACTION OF POLYPEPTIDE CHAINS OF ANTIBODIES. Proc Natl Acad Sci U S A. 1963 Oct;50:753–761. doi: 10.1073/pnas.50.4.753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. EISEN H. N., CARSTEN M. E., BELMAN S. Studies of hypersensitivity to low molecular weight substances. III. The 2,4-dinitrophenyl group as a determinant in the preciptin reaction. J Immunol. 1954 Nov;73(5):296–308. [PubMed] [Google Scholar]
  4. EISEN H. N. PREPARATION OF PURIFIED ANTI-2,4-DINITROPHENYL ANTIBODIES. Methods Med Res. 1964;10:94–102. [PubMed] [Google Scholar]
  5. EISEN H. N., SISKIND G. W. VARIATIONS IN AFFINITIES OF ANTIBODIES DURING THE IMMUNE RESPONSE. Biochemistry. 1964 Jul;3:996–1008. doi: 10.1021/bi00895a027. [DOI] [PubMed] [Google Scholar]
  6. FRANKLIN E. C., FUDENBERG H. H. ANTIGENIC HETEROGENEITY OF HUMAN RH ANTIBODIES, RHEUMATOID FACTORS, AND COLD AGGLUTININS. Arch Biochem Biophys. 1964 Mar;104:433–437. doi: 10.1016/0003-9861(64)90486-2. [DOI] [PubMed] [Google Scholar]
  7. Green I., Vassalli P., Nussenzweig V., Benacerraf B. Specificity of the antibodies produced by single cells following immunization with antigens bearing two types of antigenic determinants. J Exp Med. 1967 Mar 1;125(3):511–526. doi: 10.1084/jem.125.3.511. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hong R., Nisonoff A. Heterogeneity in the complementation of polypeptide subunits of a purified antibody isolated from an individual rabbit. J Immunol. 1966 Apr;96(4):622–628. [PubMed] [Google Scholar]
  9. LEDDY J. P., BAKEMEIER R. F. STRUCTURAL ASPECTS OF HUMAN ERYTHROCYTE AUTOANTIBODIES. I. L CHAIN TYPES AND ELECTROPHORETIC DISPERSION. J Exp Med. 1965 Jan 1;121:1–17. doi: 10.1084/jem.121.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lamm M. E., Nussenzweig V., Benacerraf B. Isolation of purified H and L polypeptide chains from guinea-pig gamma-2-immunoglobulin after mild reduction. Immunology. 1966 Apr;10(4):309–319. [PMC free article] [PubMed] [Google Scholar]
  11. MANNIK M., KUNKEL H. G. LOCALIZATION OF ANTIBODIES IN GROUP I AND GROUP II GAMMA-GLOBULINS. J Exp Med. 1963 Nov 1;118:817–826. doi: 10.1084/jem.118.5.817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. NISONOFF A. ENZYMATIC DIGESTION OF RABBIT GAMMA GLOBULIN AND ANTIBODY AND CHROMATOGRAPHY OF DIGESTION PRODUCTS. Methods Med Res. 1964;10:134–141. [PubMed] [Google Scholar]
  13. NUSSENZWEIG V., BENACERRAF B. STUDIES ON THE PROPERTIES OF FRAGMENTS OF GUINEA PIG GAMMA-1 AND GAMMA-2 ANTIBODIES OBTAINED BY PAPAIN DIGESTION AND MILD REDUCTION. J Immunol. 1964 Dec;93:1008–1014. [PubMed] [Google Scholar]
  14. Nussenzweig V., Benacerraf B. Presence of identical antigenic determinants in the Fd fragments of gamma-1- and gamma-2-guinea pig immunoglobulins. J Immunol. 1966 Aug;97(2):171–176. [PubMed] [Google Scholar]
  15. Nussenzweig V., Benacerraf B. Quantitative variations in L chain types in guinea pig antihapten antibodies. J Exp Med. 1966 Nov 1;124(5):805–818. doi: 10.1084/jem.124.5.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nussenzweig V., Lamm M. E., Benacerraf B. Presence of two types of L polypeptide chains in guinea pig 7S immunoglobulins. J Exp Med. 1966 Nov 1;124(5):787–803. doi: 10.1084/jem.124.5.787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. OETTGEN H. F., BINAGHI R. A., BENACERRAF B. HEXOSE CONTENT OF GUINEA PIG GAMMA-1 AND GAMMA-2 IMMUNOGLOBULINS. Proc Soc Exp Biol Med. 1965 Feb;118:336–342. [PubMed] [Google Scholar]
  18. ROHOLT O., ONOUE K., PRESSMAN D. SPECIFIC COMBINATION OF H AND L CHAINS OF RABBIT GAMMA-GLOBULINS. Proc Natl Acad Sci U S A. 1964 Feb;51:173–178. doi: 10.1073/pnas.51.2.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Siskind G. W., Paul W. E., Benacerraf B. Studies on the effect of the carrier molecule on antihapten antibody synthesis. I. Effect of carrier on the nature of the antibody synthesized. J Exp Med. 1966 Apr 1;123(4):673–688. doi: 10.1084/jem.123.4.673. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES