Skip to main content
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1961 Apr;40(4):636–642. doi: 10.1172/JCI104295

THE EFFECT OF IN VIVO AGING OF NORMAL HUMAN ERYTHROCYTES AND ERYTHROCYTE MACROMOLECULES UPON OXYHEMOGLOBIN DISSOCIATION*

Miles J Edwards 1,, Robert D Koler 1, Demetrios A Rigas 1, Donald M Pitcairn 1
PMCID: PMC290768  PMID: 16695857

Full text

PDF
639

Selected References

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

  1. ALLISON A. C., BURN G. P. Enzyme activity as a function of age in the human erythrocyte. Br J Haematol. 1955 Jul;1(3):291–303. doi: 10.1111/j.1365-2141.1955.tb05511.x. [DOI] [PubMed] [Google Scholar]
  2. BERNSTEIN R. E. Alterations in metabolic energetics and cation transport during aging of red cells. J Clin Invest. 1959 Sep;38:1572–1586. doi: 10.1172/JCI103936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BJORK V. O., HILTY H. J. Microvolumetric determination of CO2 and O2 tensions in arterial blood. J Appl Physiol. 1954 Jun;6(12):800–808. doi: 10.1152/jappl.1954.6.12.800. [DOI] [PubMed] [Google Scholar]
  4. BORUN E. R., FIGUEROA W. G., PERRY S. M. The distribution of Fe59 tagged human erythrocytes in centrifuged specimens as a function of cell age. J Clin Invest. 1957 May;36(5):676–679. doi: 10.1172/JCI103468. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BURKE J. D. The effects of different salt concentrations on the affinity of hemoglobin for oxygen. J Cell Comp Physiol. 1959 Aug;54:126–128. doi: 10.1002/jcp.1030540114. [DOI] [PubMed] [Google Scholar]
  6. Barcroft J., Bock A. V., Hill A. V., Parsons T. R., Parsons W., Shoji R. On the hydrogen-ion concentration and some related properties of normal human blood. J Physiol. 1922 May 16;56(3-4):157–178. doi: 10.1113/jphysiol.1922.sp001999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Barcroft J., Camis M. The dissociation curve of blood. J Physiol. 1909 Aug 26;39(2):118–142. doi: 10.1113/jphysiol.1909.sp001330. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. CROSBY W. H., MUNN J. I., FURTH F. W. Standardizing a method for clinical hemoglobinometry. U S Armed Forces Med J. 1954 May;5(5):693–703. [PubMed] [Google Scholar]
  9. HOREJSI J., KOMARKOVA A. The effect of SH-groups on the affinity of haemoglobin to oxygen. Clin Chim Acta. 1958 Mar;3(2):131–136. doi: 10.1016/0009-8981(58)90070-6. [DOI] [PubMed] [Google Scholar]
  10. HOREJSI J., KOMARKOVA A. The influence of some factors of the red blood cells on the oxygen-binding capacity of haemoglobin. Clin Chim Acta. 1960 May;5:392–395. doi: 10.1016/0009-8981(60)90144-3. [DOI] [PubMed] [Google Scholar]
  11. KAPPEST P., SCHLEGEL B. Untersuchungen zur intravitalen Erythrocytolyse. Klin Wochenschr. 1956 Aug 1;34(29-30):805–807. doi: 10.1007/BF01468052. [DOI] [PubMed] [Google Scholar]
  12. KUNKEL H. G., BEARN A. G. Minor hemoglobin components of normal human blood. Fed Proc. 1957 Sep;16(3):760–762. [PubMed] [Google Scholar]
  13. LOHR G. W., WALLER H. D., KARGES O., SCHLEGEL B., MULLER A. A. Zur Biochemie der Alterung menschlicher Erythrocyten. Klin Wochenschr. 1958 Nov 1;36(21):1008–1013. doi: 10.1007/BF01487970. [DOI] [PubMed] [Google Scholar]
  14. MARKS P. A., JOHNSON A. B. Relationship between the age of human erythrocytes and their osmotic resistance: a basis for separating young and old erythrocytes. J Clin Invest. 1958 Nov;37(11):1542–1548. doi: 10.1172/JCI103746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MURAYAMA M. Conformational differences of mercapto groups of four hemoglobins. Fed Proc. 1957 Sep;16(3):756–759. [PubMed] [Google Scholar]
  16. Marks P. A., Johnson A. B., Hirschberg E. EFFECT OF AGE ON THE ENZYME ACTIVITY IN ERYTHROCYTES. Proc Natl Acad Sci U S A. 1958 Jun;44(6):529–536. doi: 10.1073/pnas.44.6.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. PRANKERD T. A. The ageing of red cells. J Physiol. 1958 Sep 23;143(2):325–331. doi: 10.1113/jphysiol.1958.sp006062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pauling L. The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation. Proc Natl Acad Sci U S A. 1935 Apr;21(4):186–191. doi: 10.1073/pnas.21.4.186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. RIGAS D. A., KOLER R. D., OSGOOD E. E. Hemoglobin H; clinical, laboratory, and genetic studies of a family with a previously undescribed hemoglobin. J Lab Clin Med. 1956 Jan;47(1):51–64. [PubMed] [Google Scholar]
  20. RIGGS A. F. Sulfhydryl groups and the interaction between the hemes in hemoglobin. J Gen Physiol. 1952 May;36(1):1–16. doi: 10.1085/jgp.36.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. RIGGS A. F., WOLBACH R. A. Sulfhydryl groups and the structure of hemoglobin. J Gen Physiol. 1956 Mar 20;39(4):585–605. doi: 10.1085/jgp.39.4.585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. SCHLEGEL B. Agglutination der durch Isoantikörper inagglutinablen Erythrocyten mit Hilfe von Phytagglutininen. Klin Wochenschr. 1957 Jul 1;35(13):680–682. doi: 10.1007/BF01481270. [DOI] [PubMed] [Google Scholar]
  23. SIMON E. R., TOPPER Y. J. Fractionation of human erythrocytes on the basis of their age. Nature. 1957 Nov 30;180(4596):1211–1212. doi: 10.1038/1801211a0. [DOI] [PubMed] [Google Scholar]
  24. VALTIS D. J., BAIKIE A. G. The influence of red-cell thickness on the oxygen dissociation curve of blood. Br J Haematol. 1955 Apr;1(2):146–154. doi: 10.1111/j.1365-2141.1955.tb05496.x. [DOI] [PubMed] [Google Scholar]
  25. WALLER H. D., SCHLEGEL B., MUELLER A. A., LOEHR G. W. [Hemoglobin content in aging erythrocytes]. Klin Wochenschr. 1959 Sep 1;37:898–900. doi: 10.1007/BF01478505. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES