Skip to main content
NCBI 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
. 1967 Jan;57(1):39–43. doi: 10.1073/pnas.57.1.39

The solubilization of deoxyhemoglobin S.

E M Kosower, N S Kosower, P C LaCourse
PMCID: PMC335461  PMID: 5230445

Full text

PDF
39

Images in this article

41Image
on p.41

Selected References

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

  1. BARRERAS L., DIGGS L. W. BICARBONATES, PH AND PERCENTAGE OF SICKLED CELLS IN VENOUS BLOOD OF PATIENTS IN SICKLE CELL CRISIS. Am J Med Sci. 1964 Jun;247:710–718. doi: 10.1097/00000441-196406000-00012. [DOI] [PubMed] [Google Scholar]
  2. BEUTLER E. The effect of methemoglobin formation in sickle cell disease. J Clin Invest. 1961 Oct;40:1856–1871. doi: 10.1172/JCI104410. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GREENBERG M. S., KASS E. H. Studies on the destruction of red blood cells. XIII. Observations on the role of pH in the pathogenesis and treatment of painful crisis in sickle-cell disease. AMA Arch Intern Med. 1958 Feb;101(2):355–363. doi: 10.1001/archinte.1958.00260140187028. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. HAYNIE T. P., DOBSON H. L., HETTIG R. A. Molecular diseases of hemoglobin. I. Introduction and incidence. Ann Intern Med. 1957 Jun;46(6):1031–1038. doi: 10.7326/0003-4819-46-6-1031. [DOI] [PubMed] [Google Scholar]
  6. HILL R. L., SWENSON R. T., SCHWARTZ H. C. Characterization of a chemical abnormality in hemoglobin G. J Biol Chem. 1960 Nov;235:3182–3187. [PubMed] [Google Scholar]
  7. HILSCHMANN N., BRAUNITZER G. [On the N-terminal sequence of the beta-chain of human hemoglobin]. Hoppe Seylers Z Physiol Chem. 1959;317:285–287. doi: 10.1515/bchm2.1959.317.1.285. [DOI] [PubMed] [Google Scholar]
  8. HUNT J. A., INGRAM V. M. A terminal peptide sequence of human haemoglobin? Nature. 1959 Aug 22;184(Suppl 9):640–641. doi: 10.1038/184640b0. [DOI] [PubMed] [Google Scholar]
  9. Hathorn M., Lewis R. A. Inhibition of sickling by phenothiazines. Effect on red-cell survival. Br J Haematol. 1966 Mar;12(2):195–201. doi: 10.1111/j.1365-2141.1966.tb05625.x. [DOI] [PubMed] [Google Scholar]
  10. INGRAM V. M. Abnormal human haemoglobins. I. The comparison of normal human and sickle-cell haemoglobins by fingerprinting. Biochim Biophys Acta. 1958 Jun;28(3):539–545. doi: 10.1016/0006-3002(58)90516-x. [DOI] [PubMed] [Google Scholar]
  11. ITANO H. A. Solubilities of naturally occurring mixtures of human hemoglobin. Arch Biochem Biophys. 1953 Nov;47(1):148–159. doi: 10.1016/0003-9861(53)90444-5. [DOI] [PubMed] [Google Scholar]
  12. Kosower E. M. The therapeutic possibilities arising from the chemical modification of proteins. Proc Natl Acad Sci U S A. 1965 May;53(5):897–901. doi: 10.1073/pnas.53.5.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. MURAYAMA M. A MOLECULAR MECHANISM OF SICKLED ERYTHROCYTE FORMATION. Nature. 1964 Apr 18;202:258–260. doi: 10.1038/202258a0. [DOI] [PubMed] [Google Scholar]
  14. 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]

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