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. 1964 Oct;52(4):1099–1106. doi: 10.1073/pnas.52.4.1099

RECOVERY OF ANTIGENIC SPECIFICITY AFTER DENATURATION AND COMPLETE REDUCTION OF DISULFIDES IN A PAPAIN FRAGMENT OF ANTIBODY*

Edgar Haber 1,2
PMCID: PMC300401  PMID: 14224389

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Selected References

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

  1. ANFINSEN C. B., HABER E. Studies on the reduction and re-formation of protein disulfide bonds. J Biol Chem. 1961 May;236:1361–1363. [PubMed] [Google Scholar]
  2. BENNETT J. C., HABER E. Studies on antigen conformation during antibody purification. J Biol Chem. 1963 Apr;238:1362–1366. [PubMed] [Google Scholar]
  3. BUCKLEY C. E., 3rd, WHITNEY P. L., TANFORD C. THE UNFOLDING AND RENATURATION OF A SPECIFIC UNIVALENT ANTIBODY FRAGMENT. Proc Natl Acad Sci U S A. 1963 Nov;50:827–834. doi: 10.1073/pnas.50.5.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COLE R. D., STEIN W. H., MOORE S. On the cysteine content of human hemoglobin. J Biol Chem. 1958 Dec;233(6):1359–1363. [PubMed] [Google Scholar]
  5. CRUMPTON M. J., WILKINSON J. M. AMINO ACID COMPOSITIONS OF HUMAN AND RABBIT GAMMA-GLOBULINS AND OF THE FRAGMENTS PRODUCED BY REDUCTION. Biochem J. 1963 Aug;88:228–234. doi: 10.1042/bj0880228. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. EPSTEIN C. J., ANFINSEN C. B. The reversible reduction of disulfide bonds in trypsin and ribonuclease coupled to carboxymethyl cellulose. J Biol Chem. 1962 Jul;237:2175–2179. [PubMed] [Google Scholar]
  8. 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]
  9. FRATTALI V., STEINER R. F., MILLAR D. B., EDELHOCH H. REDUCTION AND REOXIDATION OF THE DISULPHIDE BONDS OF PEPSINOGEN. Nature. 1963 Sep 21;199:1186–1187. doi: 10.1038/1991186a0. [DOI] [PubMed] [Google Scholar]
  10. GOLDBERGER R. F., EPSTEIN C. J. CHARACTERIZATION OF THE ACTIVE PRODUCT OBTAINED BY OXIDATION OF REDUCED LYSOZYME. J Biol Chem. 1963 Sep;238:2988–2991. [PubMed] [Google Scholar]
  11. HABER E., ANFINSEN C. B. Side-chain interactions governing the pairing of half-cystine residues in ribonuclease. J Biol Chem. 1962 Jun;237:1839–1844. [PubMed] [Google Scholar]
  12. HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
  13. ISEMURA T., TAKAGI T., MAEDA Y., YUTANI K. Recovery of the intact structure of Taka-amylase A after reduction of all disulfide linkages in 8 M urea. J Biochem. 1963 Feb;53:155–161. doi: 10.1093/oxfordjournals.jbchem.a127671. [DOI] [PubMed] [Google Scholar]
  14. KIELLEY W. W., HARRINGTON W. F. A model for the myosin molecule. Biochim Biophys Acta. 1960 Jul 15;41:401–421. doi: 10.1016/0006-3002(60)90037-8. [DOI] [PubMed] [Google Scholar]
  15. LEVINTHAL C., SIGNER E. R., FETHEROLF K. Reactivation and hybridization of reduced alkaline phosphatase. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1230–1237. doi: 10.1073/pnas.48.7.1230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. SELA M., LIFSON S. The reformation of disulfide bridges in proteins. Biochim Biophys Acta. 1959 Dec;36:471–478. doi: 10.1016/0006-3002(59)90188-x. [DOI] [PubMed] [Google Scholar]
  19. SHECHTER E., BLOUT E. R. AN ANALYSIS OF THE OPTICAL ROTATORY DISPERSION OF POLYPEPTIDES AND PROTEINS. Proc Natl Acad Sci U S A. 1964 Apr;51:695–702. doi: 10.1073/pnas.51.4.695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SHECHTER E., CARVER J. P., BLOUT E. R. AN ANALYSIS OF THE OPTICAL ROTATORY DISPERSION OF POLYPEPTIDES AND PROTEINS, 3. Proc Natl Acad Sci U S A. 1964 Jun;51:1029–1036. doi: 10.1073/pnas.51.6.1029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. WHITE F. H., Jr Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease. J Biol Chem. 1961 May;236:1353–1360. [PubMed] [Google Scholar]
  22. WINKLER M., DOTY P. Some observations on the configuration and precipitating activity of antibodies. Biochim Biophys Acta. 1961 Dec 23;54:448–454. doi: 10.1016/0006-3002(61)90084-1. [DOI] [PubMed] [Google Scholar]
  23. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

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