Skip to main content
PMC home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1961 Jun;40(6):914–924. doi: 10.1172/JCI104330

SUBSTANCES STIMULATING GLUCOSE CATABOLISM BY THE OXIDATIVE REACTIONS OF THE PENTOSE PHOSPHATE PATHWAY IN HUMAN ERYTHROCYTES*

Arieh Szeinberg 1,†, Paul A Marks 1
PMCID: PMC290807  PMID: 13774526

Full text

PDF

Selected References

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

  1. AVRON M., JAGENDORF A. T. A TPNH diaphorase from chloroplasts. Arch Biochem Biophys. 1956 Dec;65(2):475–490. doi: 10.1016/0003-9861(56)90207-7. [DOI] [PubMed] [Google Scholar]
  2. BENESCH R. E., BENESCH R. Relation between erythrocyte integrity and sulfhydryl groups. Arch Biochem Biophys. 1954 Jan;48(1):38–42. doi: 10.1016/0003-9861(54)90302-1. [DOI] [PubMed] [Google Scholar]
  3. BEUTLER E., ROBSON M., BUTTENWIESER E. The mechanism of glutathione destruction and protection in drug-sensitive and non-sensitive erythrocytes; in vitro studies. J Clin Invest. 1957 Apr;36(4):617–628. doi: 10.1172/JCI103461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BEUTLER E. The hemolytic effect of primaquine and related compounds: a review. Blood. 1959 Feb;14(2):103–139. [PubMed] [Google Scholar]
  5. BRIN M., YONEMOTO R. H. Stimulation of the glucose oxidative pathway in human erythrocytes by methylene blue. J Biol Chem. 1958 Jan;230(1):307–317. [PubMed] [Google Scholar]
  6. BRUNS F. H., HORN H. D. Quantitative Bestimmung von L(+)-Milchsäure mit Milchsäuredehydrogenase. Biochim Biophys Acta. 1956 Aug;21(2):378–380. doi: 10.1016/0006-3002(56)90023-3. [DOI] [PubMed] [Google Scholar]
  7. CAHILL G. F., Jr, HASTINGS A. B., ASHMORE J., ZOTTU S. Studies on carbohydrate metabolism in rat liver slices. X. Factors in the regulation of pathways of glucose metabolism. J Biol Chem. 1958 Jan;230(1):125–135. [PubMed] [Google Scholar]
  8. DE DUVE C., HERS H. G. Carbohydrate metabolism. Annu Rev Biochem. 1957;26:149–180. doi: 10.1146/annurev.bi.26.070157.001053. [DOI] [PubMed] [Google Scholar]
  9. DESFORGES J. F., KALAW E., GILCHRIST P. Inhibition of glucose-6-phosphate dehydrogenase by hemolysis inducing drugs. J Lab Clin Med. 1960 May;55:757–766. [PubMed] [Google Scholar]
  10. DICKENS F. Recent advances in knowledge of the hexose monophosphate shunt. Ann N Y Acad Sci. 1958 Oct 13;75(1):71–94. doi: 10.1111/j.1749-6632.1958.tb36852.x. [DOI] [PubMed] [Google Scholar]
  11. FEGLER G. Relationship between reduced glutathione content and spontaneous haemolysis in shed blood. Nature. 1952 Oct 11;170(4328):624–625. doi: 10.1038/170624a0. [DOI] [PubMed] [Google Scholar]
  12. GREEN M. L. Reiner, chemist and medical scientist. Science. 1956 Sep 7;124(3219):434–434. doi: 10.1126/science.124.3219.434. [DOI] [PubMed] [Google Scholar]
  13. HOLZER H. Carbohydrate metabolism. Annu Rev Biochem. 1959;28:171–222. doi: 10.1146/annurev.bi.28.070159.001131. [DOI] [PubMed] [Google Scholar]
  14. HOLZER H., WITT I. [Acceleration of the oxidative pentose phosphate cycle in yeast cells by ammonium salts]. Biochim Biophys Acta. 1960 Feb 12;38:163–164. doi: 10.1016/0006-3002(60)91214-2. [DOI] [PubMed] [Google Scholar]
  15. HORECKER B. L., HIATT H. H. Pathways of carbohydrate metabolism in normal and neoplastic cells. N Engl J Med. 1958 Jan 23;258(4):177–contd. doi: 10.1056/NEJM195801232580406. [DOI] [PubMed] [Google Scholar]
  16. HORECKER B. L., SMYRNIOTIS P. Z. Phosphogluconic acid dehydrogenase from yeast. J Biol Chem. 1951 Nov;193(1):371–381. [PubMed] [Google Scholar]
  17. JANDL J. H., ENGLE L. K., ALLEN D. W. Oxidative hemolysis and precipitation of hemoglobin. I. Heinz body anemias as an acceleration of red cell aging. J Clin Invest. 1960 Dec;39:1818–1836. doi: 10.1172/JCI104206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. KIMBRO E. L., Jr, SACHS M. V., TORBERT J. V. Mechanism of the hemolytic anemia induced by nitrofurantoin (furadantin); further observations on the incidence and significance of primaquine-sensitive red cells. Bull Johns Hopkins Hosp. 1957 Nov;101(5):245–257. [PubMed] [Google Scholar]
  19. KINOSHITA J. H. The stimulation of the phosphogluconate oxidation pathway by pyruvate in bovine corneal epithelium. J Biol Chem. 1957 Sep;228(1):247–253. [PubMed] [Google Scholar]
  20. KIRKMAN H. N. Charasteristics of glucose-6-phosphate dehydrogenase from normal and primaquine-sensitive erythrocytes. Nature. 1959 Oct 24;184:1291–1292. doi: 10.1038/1841291a0. [DOI] [PubMed] [Google Scholar]
  21. Lemberg R., Legge J. W., Lockwood W. H. Coupled oxidation of ascorbic acid and haemoglobin: Quantitative studies on choleglobin formation. Estimation of haemoglobin and ascorbic acid oxidations. Biochem J. 1941 Mar;35(3):339–352. doi: 10.1042/bj0350339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. MARKS P. A., GELLHORN A., KIDSON C. Lipid synthesis in human leukocytes, platelets, and erythrocytes. J Biol Chem. 1960 Sep;235:2579–2583. [PubMed] [Google Scholar]
  23. MARKS P. A., GROSS R. T. Erythrocyte glucose-6-phosphate dehydrogenase deficiency: evidence of differences between Negroes and Caucasians with respect to this genetically determined trait. J Clin Invest. 1959 Dec;38:2253–2262. doi: 10.1172/JCI104006. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. MARKS P. A. Red cell glucose-6-phosphate and 6-phosphogluconic dehydrogenases and nucleoside phosphorylase. Science. 1958 Jun 6;127(3310):1338–1339. doi: 10.1126/science.127.3310.1338. [DOI] [PubMed] [Google Scholar]
  25. MARKS P. A., SZEINBERG A., BANKS J. Erythrocyte glucose 6-phosphate dehydrogenase of normal and mutant human subjects: properties of the purified enzymes. J Biol Chem. 1961 Jan;236:10–17. [PubMed] [Google Scholar]
  26. MELA C., PERONA G. P. Sulla resistenza in vitro del glutatione ridotto eritrocitario al succo di fave fresche; nota preventiva. Boll Soc Ital Biol Sper. 1959 Feb 15;35(3):146–148. [PubMed] [Google Scholar]
  27. MILLS G. C. Glutathione peroxidase and the destruction of hydrogen peroxide in animal tissues. Arch Biochem Biophys. 1960 Jan;86:1–5. doi: 10.1016/0003-9861(60)90357-x. [DOI] [PubMed] [Google Scholar]
  28. MILLS G. C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem. 1957 Nov;229(1):189–197. [PubMed] [Google Scholar]
  29. MILLS G. C., RANDALL H. P. Hemoglobin catabolism. II. The protection of hemoglobin from oxidative breakdown in the intact erythrocyte. J Biol Chem. 1958 Jun;232(2):589–598. [PubMed] [Google Scholar]
  30. MILLS G. C. The purification and properties of glutathione peroxidase of erythrocytes. J Biol Chem. 1959 Mar;234(3):502–506. [PubMed] [Google Scholar]
  31. MURPHY J. R. Erythrocyte metabolism. II. Glucose metabolism and pathways. J Lab Clin Med. 1960 Feb;55:286–302. [PubMed] [Google Scholar]
  32. 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]
  33. RALL T. W., LEHNINGER A. L. Glutathione reductase of animal tissues. J Biol Chem. 1952 Jan;194(1):119–130. [PubMed] [Google Scholar]
  34. RUBINSTEIN D., OTTOLENGHI P., DENSTEDT O. F. The metabolism of the erythrocyte. XIII. Enzyme activity in the reticulocyte. Can J Biochem Physiol. 1956 Mar;34(2):222–235. [PubMed] [Google Scholar]
  35. SAIFER A., GERSTENFELD S. The photometric microdetermination of blood glucose with glucose oxidase. J Lab Clin Med. 1958 Mar;51(3):448–460. [PubMed] [Google Scholar]
  36. SCOTT E. M., GRIFFITH I. V. The enzymic defect of hereditary methemoglobinemia: diaphorase. Biochim Biophys Acta. 1959 Aug;34:584–586. doi: 10.1016/0006-3002(59)90324-5. [DOI] [PubMed] [Google Scholar]
  37. STEIN W. H., MOORE S. The free amino acids of human blood plasma. J Biol Chem. 1954 Dec;211(2):915–926. [PubMed] [Google Scholar]
  38. SZEINBERG A., ADAM A., RAMOT B., SHEBA C., MYERS F. The incorporation of isotopically labelled glycine into glutathione of erythrocytes with glucose-6-phosphate dehydrogenase deficiency. Biochim Biophys Acta. 1959 Nov;36:65–73. doi: 10.1016/0006-3002(59)90070-8. [DOI] [PubMed] [Google Scholar]
  39. WALKER D. G., BOWMAN J. E. In vitro effect of Vicia faba extracts upon reduced glutathione of erythrocytes. Proc Soc Exp Biol Med. 1960 Mar;103:476–477. doi: 10.3181/00379727-103-25564. [DOI] [PubMed] [Google Scholar]
  40. WENNER C. E. Oxidation of reduced triphosphopyridine nucleotide by ascites tumor cells. J Biol Chem. 1959 Sep;234:2472–2479. [PubMed] [Google Scholar]
  41. WROBLEWSKI F., LADUE J. S. Lactic dehydrogenase activity in blood. Proc Soc Exp Biol Med. 1955 Oct;90(1):210–213. doi: 10.3181/00379727-90-21985. [DOI] [PubMed] [Google Scholar]
  42. ZINKHAM W. H., CHILDS B. A defect of glutathione metabolism in erythrocytes from patients with a naphthalene-induced hemolytic anemia. Pediatrics. 1958 Sep;22(3):461–471. [PubMed] [Google Scholar]

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

RESOURCES