Hemolytic effect of primaquine. XVI. Glyoxalase activity of primaquine-sensitive and normal erythrocytes

References

1. • Childs B.
   • Zinkham W.H.
   The Genetics of Primaquine Sensitivity of the Erythrocytes.
   in: Ciba Foundation Symposium on Biochemistry of Human Genetics. Little, Brown & Co, Boston1959: 76
   • Google Scholar
2. • Carson P.E.
   • Flanagan C.L.
   • Ickes C.E.
   • Alving A.S.
   Enzymatic Deficiency in Primaquine-Sensitive Erythrocytes.
   Science. 1956; 124: 484
   • Google Scholar
3. • Beutler E.
   • Dern B.J.
   • Flanagan C.L.
   • Alving A.S.
   The Hemolytic Effect of Primaquine. VII. Biochemical Studies of Drug-Sensitive Erythrocytes.
   J. Lab. & Clin. Med. 1955; 45: 286
   • Google Scholar
4. • Brewer G.J.
   • Tarlov A.R.
   • Kellermeyer R.W.
   The Hemolytic Effect of Primaquine. XII. Shortened Erythrocyte Life Span in Primaquine-Sensitive Male Negroes in the Absence of Drug Administration.
   J. Lab. & Clin. Med. 1961; 58: 217
   • Google Scholar
5. • Dern R.J.
   • Weinstein I.M.
   • LeRoy G.V.
   • Talmage D.W.
   • Alving A.S.
   The Hemolytic Effect of Primaquine. I. The Localization of the Drug-Induced Hemolytic Defect in Primaquine-Sensitive Individuals.
   J. Lab. & Clin. Med. 1954; 43: 303
   • Google Scholar
6. • Dern R.J.
   • Beutler E.
   • Alving A.S.
   The Hemolytic Effect of Primaquine. V. Primaquine Sensitivity as a Manifestation of a Multiple Drug Sensitivity.
   J. Lab. & Clin. Med. 1955; 45: 30
   • Google Scholar
7. • Emerson C.P.
   • Ham T.H.
   • Castle W.B.
   The Influence of Resonating Organic Compounds on the Integrity of Red Cells.
   in: Conference on the Preservation of the Formed Elements and of the Proteins of the Blood. American National Red Cross, Washington, D. C1949: 114
   • Google Scholar
8. • Alving A.S.
   • Tarlov A.R.
   • Brewer G.J.
   • Carson P.E.
   • Long W.K.
   Glucose-6-Phosphate Dehydrogenase Deficiency (Primaquine Sensitivity). An Inborn Error of Metabolism.
   in: Proc. 8th Internat. Congress Hematol, Tokyo, Japan1960: 1108
   • Google Scholar
9. • Tarlov A.R.
   • Brewer G.J.
   • Carson P.E.
   • Alving A.S.
   Primaquine Sensitivity. Glucose-6-Phosphate Dehydrogenase Deficiency: An Inborn Error of Metabolism of Medical and Biological Significance.
   A. M. A. Arch. Int. Med. 1962; 109: 209
   • Google Scholar
10. • 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; 39: 1818
    • Google Scholar
11. • Allen D.W.
    • Jandl J.H.
    Oxidative Hemolysis and Precipitation of Hemoglobin. II. Role of Thiols in Oxidant Drug Action.
    J. Clin. Invest. 1961; 40: 454
    • Google Scholar
12. • Brewer G.J.
    • Tarlov A.R.
    • Kellermeyer R.W.
    • Alving A.S.
    The Hemolytic Effect of Primaquine. XV. Role of Methemoglobin.
    J. Lab. & Clin. Med. 1962; 59: 905
    • Google Scholar
13. • Harley J.D.
    • Mauer A.M.
    Studies on the Formation of Heinz Bodies. I. Methemoglobin Production and Oxyhemoglobin Destruction.
    Blood. 1960; 16: 1722
    • Google Scholar
14. • Jandl J.H.
    Editorial, The Heinz Body Hemolytic Anemias.
    A. M. A. Ann. Int. Med. 1963; 58: 702
    • Google Scholar
15. • Kellermeyer R.W.
    • Tarlov A.R.
    • Brewer G.J.
    • Carson P.E.
    • Alving A.S.
    Hemolytic Effect of Therapeutic Drugs. Clinical Considerations of the Primaquine-Type Hemolysis.
    J. A. M. A. 1962; 180: 388
    • Google Scholar
16. • Hopkins F.G.
    • Morgan E.J.
    Studies on Glyoxalase. I. A New Factor.
    Biochem. J. 1948; 42: 23
    • Google Scholar
17. • Racker E.
    The Mechanism of Action of Glyoxalase.
    J. Biol. Chem. 1951; 51: 685
    • Google Scholar
18. • Crook E.M.
    • Law K.
    Glyoxalase: The Role of the Components.
    Biochem. J. 1952; 52: 492
    • Google Scholar
19. • Lohman K.
    Beitrag zur enzymatischen Umwandlung von synthetischem Methylglyoxal in Milchsaure.
    Biochem. Zeitschr. 1932; 254: 332
    • Google Scholar
20. • Flanagan C.L.
    • Schrier S.L.
    • Carson P.E.
    • Alving A.S.
    The Hemolytic Effect of Primaquine. VIII. The Effect of Drug Administration on Parameters of Primaquine Sensitivity.
    J. Lab. & Clin. Med. 1958; 51: 600
    • Google Scholar
21. • Grunert R.R.
    • Phillips P.H.
    A Modification of the Nitroprusside Method of Analysis for Glutathione.
    Arch. Biochem. 1951; 30: 217
    • Google Scholar
22. • Glock G.E.
    • McLean P.
    Further Studies on the Properties and Assay of Glucose-6-Phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase of Rat Liver.
    Biochem. J. 1953; 55: 400
    • Google Scholar
23. • Zinkham W.H.
    • Lenhard R.E.
    Metabolic Abnormalities of Erythrocytes From Patients With Congenital Nonspherocytic Hemolytic Anemia.
    J, Pediat. 1959; 55: 319
    • Google Scholar
24. • 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; 36: 676
    • Google Scholar
25. • Davidson E.
    The Redistribution of the Red Cells on Centrifugation.
    Acta haemat. 1960; 23: 92
    • Google Scholar
26. • Rigas D.A.
    • Koler R.D.
    Ultracentrifugal Fractionation of Human Erythrocytes on the Basis of Cell Age.
    J. Lab. & Clin. Med. 1961; 58: 242
    • Google Scholar
27. • Bernstein R.E.
    Alterations in Metabolic Energetics and Cation Transport During Aging of Red Cells.
    J. Clin. Invest. 1959; 38: 1572
    • Google Scholar
28. • Klebanoff S.J.
    Glutathione Metabolism. I. The Glyoxalase Activity of Mature Mammalian Erythrocytes.
    Biochem. J. 1956; 64: 425
    • Google Scholar
29. • Fisher R.A.
    Statistical Methods for Research Workers.
    Hafner Publishing Co, New York1958
    • Google Scholar
30. • Allison A.C.
    • Burn G.P.
    Enzyme Activity as a Function of Age in the Human Erythrocyte.
    Brit. J. Haemat. 1955; 1: 291
    • Google Scholar
31. • Valentine W.N.
    • Tanaka K.R.
    The Glyoxalase Content of Human Erythrocytes and Leukocytes.
    Acta haemat. 1961; 26: 303
    • Google Scholar
32. • Schrier S.L.
    • Kellermeyer R.W.
    • Carson P.E.
    • Ickes C.E.
    • Alving A.S.
    The Hemolytic Effect of Primaquine. IX. Enzymatic Abnormalities in Primaquine-Sensitive Erythrocytes.
    J. Lab. & Clin. Med. 1958; 52: 109
    • Google Scholar
33. • Beutler E.
    • Dern R.J.
    • Alving A.S.
    The Hemolytic Effect of Primaquine. IV. The Relationship of Cell Age to Hemolysis.
    J. Lab. & Clin. Med. 1954; 44: 439
    • Google Scholar
34. • Tarlov A.R.
    • Brewer G.J.
    • Kellermeyer R.W.
    The Effect of Drug-Induced or Blood-Loss Anemia on the Biochemical Composition of Normal and Primaquine-Sensitive (G-6PD Deficient) Reticulocytes.
    (Submitted to)in: The Meeting of the Am. Soc. Hemat. Sept. 25, 1960
    • Google Scholar
35. • Salem H.M.
    Glyoxalase and Methylglyoxal in Thiamine-Deficient Rats.
    Biochem. J. 1954; 57: 227
    • Google Scholar
36. • Tonniessen E.
    • Fischer W.
    Methylglyoxal als Abbauprodukt der Glykose.
    Hoppe-Seyl Zeitschr. 1926; 161: 254
    • Google Scholar
37. • Ariyama N.
    The Formation of Methylglyoxal From Hexose Phosphate in the Presence of Tissues.
    J. Biol. Chem. 1928; 77: 395
    • Google Scholar
38. • Salem H.M.
    ed. 3. Ph.D. Thesis. University of London, 1950
    • Google Scholar
39. • Schneider E.
    • Widmann E.
    Methylglyoxal als Zwischenprodukt des Kohlenhydratabbaues.
    Klin. Wchnschr. 1930; 9: 1916
    • Google Scholar
40. • Kun E.
    Inhibition of Succinic Dehydrogenase by Methylglyoxal.
    J. Biol. Chem. 1950; 187: 289
    • Google Scholar
41. • Meyerhof O.
    Ueber die Intermediärvorgänge bei der biologischen Kohlehydratspaltung.
    Ergebnisse Enzymforschung. 1935; 4: 208
    • Google Scholar