5
Views
4
CrossRef citations to date
0
Altmetric
Original Article

The Stability of Glucose-6-Phosphate Dehydrogenase and 6-Phospho-Gluconate Dehydrogenase in Human Erythrocytes and Hemolysates During Storage

&
Pages 177-184 | Received 15 Aug 1963, Published online: 28 Aug 2009

References

  • Bartlett B. R., Shafer A. W. Phosphorylated carbohydrate intermediates of the human erythrocyte during storage in acid citrate dextrose. J. Clin. Invest 1961; 40: 1178
  • Brewer G. J., Tarlov A. R., Kellermayer R. W. The hemolytic effect of primaquine. XII. Shortened erythrocyte life span in primaquine sensitive negroes in the absence of drug administration. J. Lab. clin. Invest 1961; 58(II)217
  • Brownstone Y. S., Denstedt O. F. The pentose phosphate pathway in the human erythrocyte. III. The stability of the pentose phosphate metabolic system in preserved erythrocytes. Canad. J. Biochem 1961; 39: 545
  • Bruns F. H., Werners P. H. Dehydrogenases. Advances in clinical chemistry, H. Sobotka, C. I. Stewart, 1962; Vol. 5: 237–294, New York and London
  • Chung A. E., Langdon R. G. Human erythrocyte glucose 6-phosphate dehydrogenase (I and II). J. biol. Chem 1963; 238: 2309
  • Doktorandenkollektiv des Physiologisch-Chemischen Institutes Berlin 1960/61: Das Yerhalten von Enzymen und Substraten bei der Konservierung von Blut in verschiedenen Medien. Folia Haematol 1962; 78: 620
  • Kerppola W., Nikkilä E. A., Pitkä nen E. Serum glucose-6-phosphate dehydrogenase in the diagnosis of myocardial infarction. Acta med. scand 1960; 166: 17
  • Kirkman H. N. Glucose 6-phosphate dehydrogenase from human erythrocytes. I. Further purification and characterization. J. biol. Chem 1962; 237: 2364
  • Kirkman H. N., Hendrickson E. M. Glucose 6-phosphate dehydrogenase from human erythrocytes. II. Subactive states of the enzyme from normal persons. Ibid 1962; 237: 2371
  • Kornberg A., Horecker B. L. Glucoses-phosphate dehydrogenase. Methods in enzymology, S. P. Colowick, N. O. Kaplan, New York 1988; Vol. 1.: 323–327
  • Marks P. A. Enzyme of the pentose phosphate pathway. Methods in medical research, J. H. Quastel, Chicago 1961; Vol. 9: 4–35
  • Marks P. A. Enzyme changes during maturation and ageing of erythrocytes. Henry Ford Hospital International Symposium: Biological interaction in normal and neoplastic growth. New York 1962; 481–497
  • Marks P. A., Johnson A. B., De Bellis R., Banks J. Stability of metabolism of erythrocytes stored in vitro. Fed. Proc 1958; 17: 269
  • Marks P. A., Johnson A. B., De Bellis R., Hirschberg E. Effect of age on the enzyme activity in erythrocytes. Proc. Nat. Acad. Sci 1958; 44: 529
  • Marks P. A., Johnson A. B., De Bellis R., Szeinberg A. Stabilization and inactivation of glucose-6-phosphate dehydrogenase of normal and mutant subjects. Fed. Proc 1960; 19: 193
  • Mollison P. L., Robinson M. A. Observations on the effects of purine nucleosides on red cell preservation. Brit. J. Haematol 1959; 5: 331
  • Prankerd T. A. J. The determination of glucose 6-phosphate dehydrogenase in red cells. The Association of Clinical Pathologists' Broadsheet no. 42 (New series) 1962
  • Ramot B., Ashkenazi I., Rimon A., Adam A., Sheba C. Activation of glucose-6-phosphate dehydrogenase of enzyme-deficient subjects. II. Properties of the activator and the activation reaction. J. Clin. Invest 1961; 40: 611
  • Shafer A. W., Bartlett G. R. Effect of inosine on the post-transfusion survival of stored rabbit erythrocytes. Ibid 1960; 39: 69

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.