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
. 1965 Dec;54(6):1773–1779. doi: 10.1073/pnas.54.6.1773

Tryptic peptides from the active sites of antibody molecules.

R F Doolittle, S J Singer
PMCID: PMC300548  PMID: 5218925

Full text

PDF
1773

Selected References

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

  1. BENNETT J. C., HOOD L. E., DREYER W. J., POTTER M. EVIDENCE FOR AMINO ACID SEQUENCE DIFFERENCES AMONG PROTEINS RESEMBLING THE L-CHAIN SUBUNITS OF IMMUNOGLOBULINS. J Mol Biol. 1965 May;12:81–87. doi: 10.1016/s0022-2836(65)80284-4. [DOI] [PubMed] [Google Scholar]
  2. DAY L. A., STURTEVANT J. M., SINGER S. J. The kinetics of the reactions between antibodies to the 2,4 dinitrophenyl group and specific haptens. Ann N Y Acad Sci. 1963 May 8;103:611–625. doi: 10.1111/j.1749-6632.1963.tb53721.x. [DOI] [PubMed] [Google Scholar]
  3. EDELMAN G. M., GALLY J. A. The nature of Bence-Jones proteins. Chemical similarities to polypetide chains of myeloma globulins and normal gamma-globulins. J Exp Med. 1962 Aug 1;116:207–227. doi: 10.1084/jem.116.2.207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. FARAH F. S., KERN M., EISEN H. N. The preparation and some properties of purified antibody specific for the 2,4-dinitrophenyl group. J Exp Med. 1960 Dec 1;112:1195–1210. doi: 10.1084/jem.112.6.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FLEISCHMAN J. B., PAIN R. H., PORTER R. R. Reduction of gamma-globulins. Arch Biochem Biophys. 1962 Sep;Suppl 1:174–180. [PubMed] [Google Scholar]
  7. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fenton J. W., 2nd, Singer S. J. Affinity labeling of antibodies to the p-azophenyltrimethylammonium hapten and a structural relationship among antibody active sites of different specificities. Biochem Biophys Res Commun. 1965 Jul 26;20(3):315–320. doi: 10.1016/0006-291x(65)90366-9. [DOI] [PubMed] [Google Scholar]
  9. GITLIN D., MERLER E. A comparison of the peptides released from related rabbit antibodies by enzymatic hydrolysis. J Exp Med. 1961 Aug 1;114:217–230. doi: 10.1084/jem.114.2.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. GOLD E. F., KNIGHT K. L., HAUROWITZ F. PEPTIDE MAPS OF ANTIBODIES AGAINST AN ANTIGEN CONTAINING TWO DIFFERENT DETERMINANT GROUPS. Biochem Biophys Res Commun. 1965 Jan 4;18:76–80. doi: 10.1016/0006-291x(65)90885-5. [DOI] [PubMed] [Google Scholar]
  12. GROFF J. L., HAUROWITZ F. COMPARISON OF THE PEPTIDE MAPS OF ANTIBODIES AGAINST AN ACIDIC AND A BASIC DETERMINANT GROUP. Immunochemistry. 1964 Apr;1:31–36. doi: 10.1016/0019-2791(64)90053-9. [DOI] [PubMed] [Google Scholar]
  13. HABER E. RECOVERY OF ANTIGENIC SPECIFICITY AFTER DENATURATION AND COMPLETE REDUCTION OF DISULFIDES IN A PAPAIN FRAGMENT OF ANTIBODY. Proc Natl Acad Sci U S A. 1964 Oct;52:1099–1106. doi: 10.1073/pnas.52.4.1099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. HIRS C. H., MOORE S., STEIN W. H. Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J Biol Chem. 1956 Apr;219(2):623–642. [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. METZGER H., MANNIK M. RECOMBINATION OF ANTIBODY POLYPEPTIDE CHAINS IN THE PRESENCE OF ANTIGEN. J Exp Med. 1964 Nov 1;120:765–782. doi: 10.1084/jem.120.5.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. METZGER H., WOFSY L., SINGER S. J. AFFINITY LABELING OF THE ACTIVE SITES OF ANTIBODIES TO THE 2,4-DINITROPHENYL HAPTEN. Biochemistry. 1963 Sep-Oct;2:979–988. doi: 10.1021/bi00905a014. [DOI] [PubMed] [Google Scholar]
  19. METZGER H., WOFSY L., SINGER S. J. THE PARTICIPATION OF A AND B POLYPEPTIDE CHAINS IN THE ACTIVE SITES OF ANTIBODY MOLECULES. Proc Natl Acad Sci U S A. 1964 Apr;51:612–618. doi: 10.1073/pnas.51.4.612. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SCHOELLMANN G., SHAW E. Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry. 1963 Mar-Apr;2:252–255. doi: 10.1021/bi00902a008. [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. 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]
  23. Velick S. F., Parker C. W., Eisen H. N. EXCITATION ENERGY TRANSFER AND THE QUANTITATIVE STUDY OF THE ANTIBODY HAPTEN REACTION. Proc Natl Acad Sci U S A. 1960 Nov;46(11):1470–1482. doi: 10.1073/pnas.46.11.1470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. WOFSY L., METZGER H., SINGER S. J. Affinity labeling-a general method for labeling the active sites of antibody and enzyme molecules. Biochemistry. 1962 Nov;1:1031–1039. doi: 10.1021/bi00912a013. [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