Summary
A new glucose 6-phosphate dehydrogenase (G6PD) variant associated with chronic nonspherocytic hemolytic anemia was discovered in Japan. The patient showed hemolytic crises after upper respiratory infections. The enzyme activity was about 3.8% of the normal. The partially purified enzyme revealed slow anodal electrophoretic mobility, high Km NADP, marked thermal-instability, and increased affinity for a substrate analogue (deamino-NADP). A particular characteristic of this enzyme was a biphasic pH curve with a greatly increased activity at low pH values. From these results, this variant was clearly different from hitherto observed G6PD variants, and was designated G6PD Asahikawa.
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Beutler E (1983) Glucose-6-phosphate dehydrogenase deficiency. In: Stanbury JB, Wyngaarden JB, Fredrickson DS, Brown MS (eds) The metabolic basis of inherited disease, 5th edn. McGraw-Hill, New York, pp 1629–1653
Beutler E, Yoshida A (1973) Human glucose-6-phosphate dehydrogenase variants: a supplementary tabulation. Ann Hum Genet 37:151–155
Beutler E, Mathai CK, Smith JE (1968) Biochemical variants of glucose-6-phosphate dehydrogenase giving rise to congenital nonspherocytic hemolytic disease. Blood 31:131–150
Beutler E, Matsumoto F, Daiber A (1974) Nonspherocytic hemolytic anemia due to G-6-PD Panama. IRCS 2:1389
Busch D, Boie K (1970) Glucose-6-Phosphat-Dehydrogenase-Defekt in Deutschland. II. Eigenschaften des Enzyms (Typ “Freiburg”). Klin Wochenschr 18:74–78
Carson PE, Frischer H (1966) Glucose-6-phosphate dehydrogenase deficiency and related disorders of the pentose phosphate pathway. Am J Med 41:744–761
Dacie JV, Lewis SM (1975) Practical haematology, 5th edn. Churchill Livingstone, Edinburgh
Mathai CK, Ohno S, Beutler E (1966) Sex-linked of the glucose-6-phosphate dehydrogenase gene in Equidae. Nature 210:115–117
Mengel CE, Metz E, Yancey WS (1967) Anemia during acute infections. Arch Intern Med 119:287–290
Miwa S, Fujii H, Nakatsuji T, Ishida Y, Oda E, Kaneto A, Motokawa M, Ariga Y, Fukuchi S, Sasai S, Hiraoka K, Kashii H, Kodama T (1978) Four new electrophoretically slow-moving glucose 6-phosphate dehydrogenase variants associated with congenital nonspherocytic hemolytic anemia found in Japan: Gd(-) Kurume, Gd(-) Fukushima, Gd(-) Yamaguchi and Gd(-) Wakayama. Am J Hematol 5:131–138
Omachi A, Scott CB, Hegarty H (1969) Pyridine nucleotides in human erythrocytes in different metabolic states. Biochim Biophys Acta 184:139–147
Ramot B, Ben-Bassat I, Shchory M (1969) New glucose-6-phosphate dehydrogenase variants observed in Israel and their association with congenital nonspherocytic hemolytic disease. J Lab Clin Med 74:895–901
Rattazzi MC, Corash LM, van Zanen GE, Jaffé ER, Piomelli S (1971) G6PD deficiency and chronic hemolysis: four new mutants—relationships between clinical syndrome and enzyme kinetics. Blood 38:205–218
Tomoda A, Suzuki H, Fukuhara Y, Ueda Y, Niho K, Yoneyama Y, Kakinuma K (1984) Involvement of active oxygens released by activated leukocytes in hemolytic mechanism of G6PD deficient red cells. Acta Haematol JPN 47:189–194
WHO Scientific Group (1967) Standardization of procedures for the study of glucose-6-phosphate dehydrogenase. WHO Tech Rep Ser 366:1–53
Yoshida A (1973) Hemolytic anemia and G6PD deficiency: physiologic activity, not in vitro activity, of enzymes is related to the severity of genetic diseases. Science 179:532–537
Yoshida A, Beutler E (1978) Human glucose-6-phosphate dehydrogenase variants: a supplementary tabulation. Ann Hum Genet 41:347–355
Yoshida A, Beutler E (1983) G-6-PD variants: another up-date. Ann Hum Genet 47:25–38
Yoshida A, Beutler E, Motulsky AG (1971) Human glucose-6-phosphate dehydrogenase variants. Bull WHO 45:243–253
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Takizawa, T., Fujii, H., Takegawa, S. et al. A unique electrophoretic slow-moving glucose 6-phosphate dehydrogenase variant (G6PD Asahikawa) with a markedly acidic pH optimum. Hum Genet 68, 70–72 (1984). https://doi.org/10.1007/BF00293876
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DOI: https://doi.org/10.1007/BF00293876