Skip to main content
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
. 1968 Feb;59(2):613–619. doi: 10.1073/pnas.59.2.613

Unique features of the variable regions of Bence Jones proteins and their possible relation to antibody complementarity.

E A Kabat
PMCID: PMC224716  PMID: 5238988

Full text

PDF
613

Selected References

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

  1. Gray W. R., Dreyer W. J., Hood L. Mechanism of antibody synthesis: size differences between mouse kappa chains. Science. 1967 Jan 27;155(3761):465–467. doi: 10.1126/science.155.3761.465. [DOI] [PubMed] [Google Scholar]
  2. Hilschmann N., Craig L. C. Amino acid sequence studies with Bence-Jones proteins. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1403–1409. doi: 10.1073/pnas.53.6.1403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hilschmann N. Die chemische Struktur von zwei Bence-Jones-Proteinen (roy und Cum.) vom kappa-Typ. Hoppe Seylers Z Physiol Chem. 1967 Aug;348(8):1077–1080. [PubMed] [Google Scholar]
  4. Hood L. E., Gray W. R., Dreyer W. J. On the mechanism of antibody synthesis: a species comparison of L-chains. Proc Natl Acad Sci U S A. 1966 Apr;55(4):826–832. doi: 10.1073/pnas.55.4.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kabat E. A. The paucity of species-specific amino acid residues in the variable regions of human and mouse Bence-Jones proteins and its evolutionary and genetic implications. Proc Natl Acad Sci U S A. 1967 May;57(5):1345–1349. doi: 10.1073/pnas.57.5.1345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kronvall G. Ligand-binding sites for streptolysin O and staphylococcal protein A on different parts of the same myeloma globulin. Acta Pathol Microbiol Scand. 1967;69(4):619–621. doi: 10.1111/j.1699-0463.1967.tb03776.x. [DOI] [PubMed] [Google Scholar]
  7. Leach S. J., Némethy G., Scheraga H. A. Computation of the sterically allowed conformations of peptides. Biopolymers. 1966 Apr-May;4(4):369–407. doi: 10.1002/bip.1966.360040402. [DOI] [PubMed] [Google Scholar]
  8. Levinthal C. Molecular model-building by computer. Sci Am. 1966 Jun;214(6):42–52. doi: 10.1038/scientificamerican0666-42. [DOI] [PubMed] [Google Scholar]
  9. Metzger H. Characterization of a human macroglobulin. V. A Waldenström macroglobulin with antibody activity. Proc Natl Acad Sci U S A. 1967 May;57(5):1490–1497. doi: 10.1073/pnas.57.5.1490. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Milstein C. Chemical structure of light chains. Proc R Soc Lond B Biol Sci. 1966 Nov 22;166(1003):138–149. doi: 10.1098/rspb.1966.0089. [DOI] [PubMed] [Google Scholar]
  11. Milstein C., Clegg J. B., Jarvis J. M. C-terminal half of immunoglobulin lambda-chains. Nature. 1967 Apr 15;214(5085):270–272. doi: 10.1038/214270a0. [DOI] [PubMed] [Google Scholar]
  12. Milstein C. Linked groups of residues in immunoglobulin k chains. Nature. 1967 Oct 28;216(5113):330–332. doi: 10.1038/216330a0. [DOI] [PubMed] [Google Scholar]
  13. Milstein C. Variations in amino-acid sequence near the disulphide bridges of Bence-Jones proteins. Nature. 1966 Jan 22;209(5021):370–373. doi: 10.1038/209370a0. [DOI] [PubMed] [Google Scholar]
  14. Niall H. D., Edman P. Two structurally distinct classes of kappa-chains in human immunoglobulins. Nature. 1967 Oct 21;216(5112):262–263. doi: 10.1038/216262a0. [DOI] [PubMed] [Google Scholar]
  15. Piggot P. J., Press E. M. Cyanogen bromide cleavage and partial sequence of the heavy chain of a pathological immunoglobulin G. Biochem J. 1967 Aug;104(2):616–626. doi: 10.1042/bj1040616. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Putnam F. W., Shinoda T., Titani K., Wikler M. Immunoglobulin structure: variation in amino acid sequence and length of human lambda light chains. Science. 1967 Sep 1;157(3792):1050–1053. doi: 10.1126/science.157.3792.1050. [DOI] [PubMed] [Google Scholar]
  17. Putnam F. W., Titani K., Whitley E., Jr Chemical structure of light chains: amino acid sequence of type K Bence-Jones proteins. Proc R Soc Lond B Biol Sci. 1966 Nov 22;166(1003):124–137. doi: 10.1098/rspb.1966.0088. [DOI] [PubMed] [Google Scholar]
  18. Titani K., Whitley E., Jr, Avogardo L., Putnam F. W. Immunoglobulin structure: partial amino acid sequence of a Bence Jones protein. Science. 1965 Sep 3;149(3688):1090–1092. doi: 10.1126/science.149.3688.1090. [DOI] [PubMed] [Google Scholar]
  19. Titani K., Whitley E., Jr, Putnam F. W. Immunoglobulin structure: variation in the sequence of Bence Jones proteins. Science. 1966 Jun 10;152(3728):1513–1516. doi: 10.1126/science.152.3728.1513. [DOI] [PubMed] [Google Scholar]
  20. Titani K., Wikler M., Putnam F. W. Evolution of immunoglobulins: structural homology of kappa and lambda Bence Jones proteins. Science. 1967 Feb 17;155(3764):828–835. doi: 10.1126/science.155.3764.828. [DOI] [PubMed] [Google Scholar]
  21. Wikler M., Titani K., Shinoda T., Putnam F. W. The complete amino acid sequence of a lambda type Bence-Jones protein. J Biol Chem. 1967 Apr 10;242(7):1668–1670. [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