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
. 1958 Jun;44(6):522–529. doi: 10.1073/pnas.44.6.522

ON DISSOCIATION AND RECOMBINATION OF HUMAN ADULT HEMOGLOBINS A, S, AND C

Harvey A Itano 1,2, S J Singer 1,2
PMCID: PMC528613  PMID: 16590233

Full text

PDF
526

Images in this article

523Image
on p.523
523Image
on p.523
523Image
on p.523

Selected References

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

  1. BENESCH R. E., LARDY H. A., BENESCH R. The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins. J Biol Chem. 1955 Oct;216(2):663–676. [PubMed] [Google Scholar]
  2. FIELD E. O., O'BRIEN J. R. Dissociation of human haemoglobin at low pH. Biochem J. 1955 Aug;60(4):656–661. doi: 10.1042/bj0600656. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. FIELD E. O., OGSTON A. G. Boundary spreading in the migration of a solute in rapid dissociation equilibrium; theory and its application to the case of human haemoglobin. Biochem J. 1955 Aug;60(4):661–665. doi: 10.1042/bj0600661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GUTTER F. J., SOBER H. A., PETERSON E. A. The effect of mercaptoethanol and urea on the molecular weight of hemoglobin. Arch Biochem Biophys. 1956 Jun;62(2):427–434. doi: 10.1016/0003-9861(56)90141-2. [DOI] [PubMed] [Google Scholar]
  5. HARRIS J. W. Studies on the destruction of red blood cells. VIII. Molecular orientation in sickle cell hemoglobin solutions. Proc Soc Exp Biol Med. 1950 Oct;75(1):197–201. doi: 10.3181/00379727-75-18144. [DOI] [PubMed] [Google Scholar]
  6. INGRAM V. M. A specific chemical difference between the globins of normal human and sickle-cell anaemia haemoglobin. Nature. 1956 Oct 13;178(4537):792–794. doi: 10.1038/178792a0. [DOI] [PubMed] [Google Scholar]
  7. ITANO H. A., NEEL J. V. A new inherited abnormality of human hemoglobin. Proc Natl Acad Sci U S A. 1950 Nov;36(11):613–617. doi: 10.1073/pnas.36.11.613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. PAULING L., ITANO H. A. Sickle cell anemia a molecular disease. Science. 1949 Nov 25;110(2865):543–548. doi: 10.1126/science.110.2865.543. [DOI] [PubMed] [Google Scholar]
  9. PERUTZ R. R., LIQUORI A. M., EIRICH F. X-ray and solubility studies of the haemoglobin of sickle-cell anaemia patients. Nature. 1951 Jun 9;167(4258):929–931. doi: 10.1038/167929a0. [DOI] [PubMed] [Google Scholar]
  10. SCHROEDER W. A., KAY L. M., WELLS I. C., GERKE C., MOSS J. Amino acid composition of hemoglobins of normal Negroes and sickle-cell anemics. J Biol Chem. 1950 Nov;187(1):221–240. [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