Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1966 Feb;55(2):445–452. doi: 10.1073/pnas.55.2.445

Dependence of the chemical nature of antibodies on the net electrical charge of antigens.

M Sela, E Mozes
PMCID: PMC224164  PMID: 4161286

Full text

PDF

Images in this article

447Image
on p.447

Selected References

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

  1. BASSETT E. W., TANENBAUM S. W., PRYZWANSKY K., BEISER S. M., KABAT E. A. STUDIES ON HUMAN ANTIBODIES. 3. AMINO ACID COMPOSITION OF FOUR ANTIBODIES FROM ONE INDIVIDUAL. J Exp Med. 1965 Aug 1;122:251–261. doi: 10.1084/jem.122.2.251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BENACERRAF B., OVARY Z., BLOCH K. J., FRANKLIN E. C. Properties of guinea pig 7S antibodies. I. Electrophoretic separation of two types of guinea pig 7S antibodies. J Exp Med. 1963 Jun 1;117:937–949. doi: 10.1084/jem.117.6.937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BLOCH K. J., KOURILSKY F. M., OVARY Z., BENACERRAF B. Properties of guinea pig 7S antibodies. III. Identification of antibodies involved in complement fixation and hemolysis. J Exp Med. 1963 Jun 1;117:965–981. doi: 10.1084/jem.117.6.965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COHEN S., PORTER R. B. STRUCTURE AND BIOLOGICAL ACTIVITY OF IMMUNOGLOBULINS. Adv Immunol. 1964;27:287–349. doi: 10.1016/s0065-2776(08)60710-5. [DOI] [PubMed] [Google Scholar]
  5. CONSDEN R., KOHN J. Cellulose acetate as a medium for immuno-diffusion. Nature. 1959 May 30;183(4674):1512–1513. doi: 10.1038/1831512a0. [DOI] [PubMed] [Google Scholar]
  6. FEINSTEIN A. ELECTROPHORETIC BEHAVIOUR OF RABBIT GAMMA-GLOBULIN FRAGMENTS AND CHAINS. Nature. 1964 Jun 27;202:1298–1301. doi: 10.1038/2021298a0. [DOI] [PubMed] [Google Scholar]
  7. Fuchs S., Sela M. Preparation and characterization of poly-DL-alanyl rabbit gamma-globulin. J Biol Chem. 1965 Sep;240(9):3558–3567. [PubMed] [Google Scholar]
  8. GITLIN D., MERLER E. Similarity of peptides in two antigen-combining fragments released from a rabbit antibody by papain. Nature. 1961 May 13;190:634–635. doi: 10.1038/190634a0. [DOI] [PubMed] [Google Scholar]
  9. GIVOL D., SELA M. ISOLATION AND FRAGMENTATION OF ANTIBODIES TO POLYTYROSYL GELATIN. Biochemistry. 1964 Mar;3:444–451. doi: 10.1021/bi00891a024. [DOI] [PubMed] [Google Scholar]
  10. KOSHLAND M. E., ENGLBERGER F. M. Differences in the amino acid composition of two purified antibodies from the same rabbit. Proc Natl Acad Sci U S A. 1963 Jul;50:61–68. doi: 10.1073/pnas.50.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Koshland M. E., Englberger F. M., Shapanka R. Differences in the Amino Acid Composition of a Third Rabbit Antibody. Science. 1964 Mar 20;143(3612):1330–1331. doi: 10.1126/science.143.3612.1330. [DOI] [PubMed] [Google Scholar]
  12. LEVY H. B., SOBER H. A. A simple chromatographic method for preparation of gamma globulin. Proc Soc Exp Biol Med. 1960 Jan;103:250–252. doi: 10.3181/00379727-103-25476. [DOI] [PubMed] [Google Scholar]
  13. Mandy W. J., Stambaugh M. K., Nisonoff A. Amino Acid Composition of Univalent Fragments of Rabbit Antibody. Science. 1963 May 24;140(3569):901–903. doi: 10.1126/science.140.3569.901. [DOI] [PubMed] [Google Scholar]
  14. OVARY Z., BENACERRAF B., BLOCH K. J. Properties of guinea pig 7S antibodies. II. Identification of antibodies involved in passive cutaneous and systemic anaphylaxis. J Exp Med. 1963 Jun 1;117:951–964. doi: 10.1084/jem.117.6.951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. OVARY Z. Immediate reactions in the skin of experimental animals provoked by antibody-antigen interaction. Prog Allergy. 1958;5:459–508. [PubMed] [Google Scholar]
  16. PALMER J. L., MANDY W. J., NISONOFF A. Heterogeneity of rabbit antibody and its subunits. Proc Natl Acad Sci U S A. 1962 Jan 15;48:49–53. doi: 10.1073/pnas.48.1.49. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. PORTER R. R., PRESS E. M. Immunochemistry. Annu Rev Biochem. 1962;31:625–652. doi: 10.1146/annurev.bi.31.070162.003205. [DOI] [PubMed] [Google Scholar]
  18. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. PRESSMAN D., ROHOLT O. Isolation of peptides from an antibody site. Proc Natl Acad Sci U S A. 1961 Oct 15;47:1606–1610. doi: 10.1073/pnas.47.10.1606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reisfeld R. A., Dray S., Nisonoff A. Differences in amino acid composition of rabbit gamma-G-immunoglobulin light polypeptide chains controlled by allelic genes. Immunochemistry. 1965 Jun;2(2):155–167. doi: 10.1016/0019-2791(65)90017-0. [DOI] [PubMed] [Google Scholar]
  21. SEIJEN H. G., GRUBER M. STRUCTURE OF GAMMA-GLOBULINS AND ANTIBODIES. J Mol Biol. 1963 Aug;7:209–211. doi: 10.1016/s0022-2836(63)80047-9. [DOI] [PubMed] [Google Scholar]
  22. SELA M., FUCHS S., ARNON R. Studies on the chemical basis of the antigenicity of proteins. 5. Synthesis, characterization and immunogenicity of some multichain and linear polypeptides containing tyrosine. Biochem J. 1962 Oct;85:223–235. doi: 10.1042/bj0850223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. SELA M., GIVOL D., MOZES E. RESOLUTION OF RABBIT GAMMA-GLOBULIN INTO TWO FRACTIONS BY CHROMATOGRAPHY ON DIETHYLAMINOETHYL-SEPHADEX. Biochim Biophys Acta. 1963 Dec 13;78:649–657. doi: 10.1016/0006-3002(63)91031-x. [DOI] [PubMed] [Google Scholar]
  24. STELOS P., RADZIMSKI G., PRESSMAN D. Heterogeneity of rabbit antibody fragments. J Immunol. 1962 May;88:572–580. [PubMed] [Google Scholar]
  25. STELOS P., ROHOLT O., PRESSMAN D. Heterogeneity of the major fractions of papain digests of rabbit antibody. J Immunol. 1962 Jul;89:113–115. [PubMed] [Google Scholar]
  26. STELOS P., YAGI Y., PRESSMAN D. MULTIPLE DISCRETE COMPONENTS OF THE UNIVALENT FRAGMENTS OF RABBIT ANTIBODIES. J Immunol. 1964 Jul;93:106–113. [PubMed] [Google Scholar]
  27. Slobin L. I., Sela M. Use of urea in the purification of antibodies. Biochim Biophys Acta. 1965 Oct 18;107(3):593–596. doi: 10.1016/0304-4165(65)90202-3. [DOI] [PubMed] [Google Scholar]
  28. TERRES G., WOLINS W. Enhanced immunological sensitization of mice by the simultaneous injection of antigen and specific antiserum. I. Effect of varying the amount of antigen used relative to the antiserum. J Immunol. 1961 Apr;86:361–368. [PubMed] [Google Scholar]
  29. VANSANTEN G., LAGNAUX S., HAMERS R., JEENER R. TWO TYPES OF ANTIBODY MOLECULES OF IDENTICAL RESTRICTED SPECIFICITY REGULARLY PRESENT IN INDIVIDUAL RABBITS. Biochim Biophys Acta. 1964 Feb 10;82:433–435. doi: 10.1016/0304-4165(64)90325-3. [DOI] [PubMed] [Google Scholar]
  30. YPHANSTIS D. A. Rapid determination of molecular weights of peptides and preteins. Ann N Y Acad Sci. 1960 Aug 31;88:586–601. doi: 10.1111/j.1749-6632.1960.tb20055.x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES