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. 1965 Sep;54(3):822–830. doi: 10.1073/pnas.54.3.822

Reductive dissociation of chicken gamma-G immunoglobulin in neutral solvents without a dispersing agent.

G R Dreesman, A A Benedict
PMCID: PMC219750  PMID: 4159570

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Selected References

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

  1. BENEDICT A. A., BROWN R. J., HERSH R. T. THE TEMPORAL SYNTHESIS AND SOME CHROMATOGRAPHICAND ULTRACENTRIFUGAL CHARACTERISTICS OF CHICKEN ANTIBODIES. J Immunol. 1963 Mar;90:399–411. [PubMed] [Google Scholar]
  2. CLELAND W. W. DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS. Biochemistry. 1964 Apr;3:480–482. doi: 10.1021/bi00892a002. [DOI] [PubMed] [Google Scholar]
  3. DEUTSCH H. F., MORTON J. I. Dissociation of human serum macroglobulins. Science. 1957 Mar 29;125(3248):600–601. doi: 10.1126/science.125.3248.600. [DOI] [PubMed] [Google Scholar]
  4. DREESMAN G., LARSON C., PINCKARD R. N., GROYON R. M., BENEDICT A. A. ANTIBODY ACTIVITY IN DIFFERENT CHICKEN GLOBULINS. Proc Soc Exp Biol Med. 1965 Jan;118:292–296. doi: 10.3181/00379727-118-29823. [DOI] [PubMed] [Google Scholar]
  5. EDELMAN G. M., POULIK M. D. Studies on structural units of the gamma-globulins. J Exp Med. 1961 May 1;113:861–884. doi: 10.1084/jem.113.5.861. [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. GROSSBERG A. L., STELOS P., PRESSMAN D. Structure of fragments of antibody molecules as revealed by reduction of exposed disulfide bonds. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1203–1209. doi: 10.1073/pnas.48.7.1203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. JAQUET H., BLOOM B., CEBRA J. J. THE REDUCTIVE DISSOCIATION OF RABBIT IMMUNE GLOBULIN IN SODIUM DODECYLSULFATE. J Immunol. 1964 Jun;92:991–1007. [PubMed] [Google Scholar]
  10. 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]
  11. ROSENQUIST G. L., GILDEN R. V. CHICKEN ANTIBODIES TO BOVINE SERUM ALBUMIN. MOLECULAR SIZE AND SENSITIVITY TO 2-MERCAPTOETHANOL. Biochim Biophys Acta. 1963 Nov 15;78:543–545. doi: 10.1016/0006-3002(63)90920-x. [DOI] [PubMed] [Google Scholar]
  12. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  13. SCHUR P. H., CHRISTIAN G. D. THE ROLE OF DISULFIDE BONDS IN THE COMPLEMENT-FIXING AND PRECIPITATING PROPERTIES OF 7S RABBIT AND SHEEP ANTIBODIES. J Exp Med. 1964 Oct 1;120:531–545. doi: 10.1084/jem.120.4.531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. UHR J. W., FINKELSTEIN S., FRANKLIN E. C. Antibody response to bacteriophage phi-X-174 in non-mammalian vertebrates. Proc Soc Exp Biol Med. 1962 Oct;111:13–15. doi: 10.3181/00379727-111-27691. [DOI] [PubMed] [Google Scholar]
  15. UTSUMI S., KARUSH F. THE SUBUNITS OF PURIFIED RABBIT ANTIBODY. Biochemistry. 1964 Sep;3:1329–1338. doi: 10.1021/bi00897a024. [DOI] [PubMed] [Google Scholar]

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