Analysis of Glucose-6-Phosphate Dehydrogenase Genetic Polymorphism in the Hakka Population in Southern China
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BACKGROUND In southern China, glucose-6-phosphate dehydrogenase (G6PD) deficiency is a significant health problem. The aim of this study was to investigate the molecular epidemiological characteristic of the G6PD gene among Chinese Hakka in southern Guangdong province. MATERIAL AND METHODS We screened 611 unrelated subjects for G6PD genetic polymorphism analyzed by a gene chip analysis for common Chinese G6PD mutations. G-6-PD enzyme activity was determined by use of the G-6-PD quantitative detection kit. RESULTS Seven mutation sites were detected from subjects in our study. G6PD Canton (c.1376 G→T)(33.06%), G6PD Kaiping (c.1388 G→A)(30.67%), and polymorphism (c.1311 C→T)(25.89%) account for 89.62% of mutations, followed by G6PD Gaohe (c.95 A→G)(5.97%), G6PD Chinese-5 (c.1024 C→T)(3.58%), G6PD Maewo (c.1360 C→T)(0.39%), and G6PD Viangchan (c.871G→A)(0.39%). CONCLUSIONS We studied the genetic polymorphisms and frequencies of G6PD gene in the Hakka population of Meizhou. Our results coincide with the results among the Chinese Jiangxi Hakka population. It was consistent with previous research reports on Chinese people. There were differences in the results of reports from some other Asian populations. Our results could be useful for future prevention and control of G6PD deficiency aimed at the Chinese Hakka population.Keywords:
Southern china
Glucose-6-Phosphate Dehydrogenase Deficiency
Glutathione reductase
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A human glucose-6-phosphate dehydrogenase variant was characterized and purified. The result showed that this was a new variast which was named as Gd (-) Zhanjiang. Compared with the specific activity (163IU/mg) of the purified normal glucose-6-phosphate dehydrogenase, the specif ic activity (28IU/mg) of the purified Gd (-) Zhanjiang was lower than that of normal one and indicated that decrease in enzyme activity was the major defect of this new glucose-6-phosphate dehydrogenase variant.
Key words:
Glucose-6-phosphate dehydrogenase; purification; structure and function of enzyme; glucose-6-phosphate dehydrogenase variant
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Glucose-6-phosphate dehydrogenase (G6PD) activity and the affinity for its substrate glucose-6-phosphate were investigated under conditions similar to the physiological environment in terms of ionic strength (I: 0.188), cation concentration, pH 7.34, and temperature (37oC). A 12.4, 10.4 and 21.4% decrease was observed in G6PD B, G6PD A+ and G6PD A- activities, respectively. A Km increase of 95.1, 94.4 and 95.4% was observed in G6PD B, G6PD A+ and G6PD A-, respectively, leading to a marked decrease in affinity. In conclusion, the observation of the reduced activity and affinity for its natural substrate reflects the actual pentose pathway rate. It also suggests a much lower NADPH generation, which is crucial mostly in G6PD-deficient individuals, whose NADPH availability is poor.
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The reasons for the decreased stability of glucose-6-phosphate dehydrogenase in transformed human cells were investigated. The enzyme stability was found to be dependent on its subunit composition; the dimeric form possessed a lower stability in comparison with the tetrameric one. An addition of NADP to cell extracts which had partly lost their glucose-6-phosphate dehydrogenase activity, resulted in reactivation and stabilization of the enzyme. The constants for a forward (k1) and back (k2) reactions during stabilization are equal to 2.87 X 10(-3) and 5.77 X 10(-1) s-1, respectively. The inactivation and reactivation kinetics suggest that the enzyme destabilization may also occur inside the cells. The cells contain more than 40% of glucose-6-phosphate dehydrogenase molecules in an inactive form. A mechanism of destabilization and inactivation of glucose-6-phosphate dehydrogenase is proposed, which consists in NADP hydrolysis and enzyme decomposition to inactive monomers which are less stable to proteolysis.
Proteolysis
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ABSTRACT Glucose-6-phosphate dehydrogenase (G6PD) enzyme function and genotype were determined in Ugandan children with uncomplicated falciparum malaria enrolled in a primaquine trial after exclusion of severe G6PD deficiency by fluorescent spot test. G6PD A− heterozygotes and hemizygotes/homozygotes experienced dose-dependent lower hemoglobin concentrations after treatment. No severe anemia was observed.
Primaquine
Glucose-6-Phosphate Dehydrogenase Deficiency
Glucosephosphate Dehydrogenase Deficiency
Heterozygote advantage
Hemoglobinopathy
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Editorial Notes1 January 1968Variants of Glucose 6-Phosphate DehydrogenaseIAN H. PORTER, M.B., B.S.IAN H. PORTER, M.B., B.S.Search for more papers by this authorAuthor, Article, and Disclosure Informationhttps://doi.org/10.7326/0003-4819-68-1-250 SectionsAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinkedInRedditEmail ExcerptGlucose 6-phosphate dehydrogenase (G6PD) is the enzyme that catalyzes the first step in the pentose phosphate shunt. This enzyme attracted much medical interest when it was discovered that "primaquine sensitivity" was due to deficiency of this enzyme (1). Excitement was heightened when it was found that G6PD deficiency is an X-linked genetic condition (2, 3) and that it is common in Negroes and whites of Mediterranean origin which suggests, as in the case of the sickle cell gene, that its presence may be of some advantage.When a genetic condition is examined closely it usually turns out to be heterogeneous....References1. CARSONFLANAGANICKESALVING PECLCEAS: Enzymatic deficiency in primaquine sensitive erythrocytes. Science 124: 484, 1956. CrossrefMedlineGoogle Scholar2. CHILDSKINKHAMBROWNEKIMBOTORBERT BWHEAELJW: A genetic study of a defect in glutathione metabolism of the erythrocyte. Bull. Hopkins Hosp. 102: 21, 1958. MedlineGoogle Scholar3. PORTERSCHULZEMCKUSICK IHJVA: Genetical linkage between the loci for glucose-6-phosphate dehydrogenase deficiency and colour-blindness in American Negroes. Ann. Hum. Genet. 26: 107, 1962. CrossrefMedlineGoogle Scholar4. KIRKMANSCHETTINIPICKARD HNFBM: Mediterranean variant of glucose-6-phosphate dehydrogenase. J. Lab. Clin. Med. 63: 726, 1964. Google Scholar5. STAMATOYANNOPOULOSPANAYOTOPOULOSPAPAYANNOPOULOU GAT: Mild glucose-6-phosphate dehydrogenase deficiency in Greek males. Lancet 2: 932, 1964. CrossrefMedlineGoogle Scholar6. STAMATOYANNOPOULOSPAPAYANNOPOULOUBAKOPOULOSMOTULSKY GTCAG: Detection of glucose-6-phosphate dehydrogenase deficient heterozygotes. Blood 29: 87, 1967. CrossrefMedlineGoogle Scholar7. MARKSBANKSGROSS PAJRT: Genetic heterogeneity of glucose-6-phosphate dehydrogenase deficiency. Nature (London) 194: 454, 1962. CrossrefGoogle Scholar8. BOYERPORTERWEILBACHER SHIHRG: Electrophoretic heterogeneity of glucose-6-phosphate dehydrogenase and its relationship to enzyme deficiency in man. Proc. Nat. Acad. Sci. USA 48: 1868, 1962. CrossrefMedlineGoogle Scholar9. KIRKMANROSENTHALSIMONCARSONBRINSON HNIMERPEAG: "Chicago I" variant of glucose-6-phosphate dehydrogenase in congenital hemolytic disease. J. Lab. Clin. Med. 63: 715, 1964. MedlineGoogle Scholar10. KIRKMANRILEY HNHD: Congenital nonspherocytic hemolytic anemia. Amer. J. Dis. Child. 102: 313, 1961. CrossrefMedlineGoogle Scholar11. KIRKMANHENDRICKSON HNEM: Sex-linked electrophoretic difference in glucose-6-phosphate dehydrogenase in different populations. Amer. J. Hum. Genet. 15: 241, 1963. MedlineGoogle Scholar12. STAMATOYANNOPOULOSYOSHIDABACOPOULOSMOTULSKY GACAG: Another variant of glucose-6-phosphate dehydrogenase. Science 157: 831, 1967. CrossrefMedlineGoogle Scholar13. KAPLANROSASERINGEHOEFFEL JCRPJC: The genetic polymorphism of red cell glucose-6-phosphate dehydrogenase in man. 1st study of a slow variant with a normal activity. Enzym. Biol. Clin. (Basel) 8: 321, 1967. CrossrefMedlineGoogle Scholar14. KAPLANROSASERINGEHOEFFEL JCRPJC: The genetic polymorphism of red cell glucose-6-phosphate dehydrogenase in man. IInd study of a new variant with a diminished activity: the "Kabyle" type. Ibid., p. 332. Google Scholar15. PORTERBOYERWATSON-WILLIAMSADAMSZEINBERGSINISCOLO IHSHEJAAM: Variation of glucose-6-phosphate dehydrogenase in different populations. Lancet 1: 895, 1964. CrossrefMedlineGoogle Scholar16. Nomenclature of glucose-6-phosphate dehydrogenase in man. Bull. WHO 36: 319, 1967. MedlineGoogle Scholar17. Nomenclature of glucose-6-phosphate dehydrogenase in man. Acta Genet. (Basel) 17: 545, 1967. Google Scholar This content is PDF only. To continue reading please click on the PDF icon. Author, Article, and Disclosure InformationAuthors: IAN H. PORTER, M.B., B.S.Affiliations: Department of Pediatrics Albany Medical College Albany, N. Y. PreviousarticleNextarticle Advertisement FiguresReferencesRelatedDetails Metrics Cited byTechniques for the Separation of IsoenzymesEnzyme Multiplicity in the Glycolytic Pathway and the Pentose—Phosphate CycleTechniques for the Separation of IsoenzymesEnzyme Multiplicity in the Glycolytic Pathway and the Pentose—Phosphate Cycle 1 January 1968Volume 68, Issue 1Page: 250-252KeywordsDehydrogenasesEnzymesGeneticsGlucosePhosphatesPrimaquine ePublished: 1 December 2008 Issue Published: 1 January 1968 PDF downloadLoading ...
Glucose-6-Phosphate Dehydrogenase Deficiency
Primaquine
Glucosephosphate Dehydrogenase Deficiency
Phosphogluconate dehydrogenase
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Assistant Professor, Department of Pediatric, Faculty of Medicine, Tehran University of Medical Sciences, Ali Asghar Hospital Tehran, Iran. Associate Professor, Department of Pediatric, Faculty of Medicine, Tehran University of Medical Sciences, Ali Asghar Hospital Tehran, Iran. Pediatrician, Ali Asghar Hospital Tehran, Iran. ___________________________________________________________________________ Abstract
Glucose-6-Phosphate Dehydrogenase Deficiency
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