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At least 73 records · Page 4Linked to original sources
PubMed1998

[Expression and biochemical characterization of human G6PD gene 1376 and 1388 mutation in G6PD-deficient Escherichia coli].

Nine types of human G6PD gene mutated at the positions of nt 1376 and nt 1388 by site-directed mutagenesis were transformed into the strain of G6PD dificent E. coli HB 351(DE3). The mutated gene was expressed successfully and the enzyme kinetic studies undertaken according to WHO standardization. The results showed that the arginine residues at the positions of 459 and 463 of G6PD gene play an important role in maintaining activity of the enzyme. The amino acid structure, polarity, and electronic property may be responsible for it. The arginine residues at the positions of 459 and 463 are also important for the enzyme-NADP+ binding, but it was not interfered by the lysine-arginine substitution. By inducing a non-sense mutation, it was further demonstrated that the amino acids residueds behind the position of 459 were extremely significant for G6PD activity.

Escherichia coli↗
PubMed1977

[Genetic heterogeneity of G6PD deficiency: mutant alleles of G6PD in the Shekii district of Azerbaijan].

Examination on G6PD deficiency in 349 patients of Shekii district hospital (Azerbaijan) revealed 16 hemi-, 4 homo- and 9 heterozygotic carriers of the defect. Gd- frequency, calculated from the data obtained (7.7%), may be compared to neighbouring regions' frequencies (6-30%). Carriers of G6PD deficiency are residents of 11 villages located in Alasani-Aphtalan valley, highly endemic with malaria in the past; nearly all marriages are endogamic. Physico-chemical and kinetic study of 10 mutant forms of G6PD, according to WHO program, led to identification of 5 variants of the II class (Shekii, Bideiz, Shirin-Bulakh, Okhut I and Zakataly) and 2 variants of the III class (Okhut II and Martinique-like). Resemblance of the majority of variants in electrophoretic mobility and the level of erythrocyte enzyme activity permit to suggest the existence of a common parental mutant G6PD allele distributed in this area.

Alleles↗
PubMed1990

The NT 1311 polymorphism of G6PD: G6PD Mediterranean mutation may have originated independently in Europe and Asia.

A polymorphic site exists in exon 11 of G6PD: in the wild-type enzyme, nucleotide (NT) 1311 is a C, but is some individuals from diverse populations a T is present instead. Nine of 54 X chromosomes from Europeans of mixed origins, nine of 41 X chromosomes of Ashkenazi Jewish subjects, three of 18 X chromosomes of Sicilians, five of 20 African X chromosomes, and nine of 20 Asian Indian X chromosomes had the mutant genotype. In contrast, the mutation was found in only three of 59 Oriental X chromosomes and in three of 30 Central/South American X chromosomes. The mutation was absent from four samples of chimpanzee DNA. Twenty-one of 22 male subjects from Mediterranean countries who had the G6PD Mediterranean 563T genotype investigated in the present study or reported previously had a T at NT 1311. Only one had the normal C at NT 1311. In contrast, both G6PD Mediterranean563T males from the Indian subcontinent had the normal C at NT 1311. These findings suggest that the same mutation at nucleotide 563 giving rise to G6PD Mediterranean may have arisen independently in Europe and in Asia.

Animals↗
PubMed1993

G6PD Mediterranean accounts for the high prevalence of G6PD deficiency in Kurdish Jews.

The Jews of Kurdistan are a small inbred population with a high incidence of beta-thalassaemia and glucose-6-phosphate dehydrogenase (G6PD) deficiency. Recently, it was reported that the beta-thalassaemia in this population shows an unusual mutational diversity; 13 different mutations were identified, of which 4 had not previously been observed in any other population. In contrast, we now report that the G6PD deficiency, which has the highest known incidence in the world, and which affects about 70% of males, is almost entirely attributable to a single widespread mutation, G6PD Mediterranean.

Female↗
PubMedDate not supplied

G6PD NanKang (517 T-->C; 173 Phe-->Leu): a new Chinese G6PD variant associated with neonatal jaundice.

Using a non-radioactive PCR-SSCP technique, we identified a novel glucose-6-phosphate dehydrogenase (G6PD) mutation in a Chinese newborn with neonatal jaundice. This new variant (G6PD NanKang) causes a T to C change at nucleotide position 517, producing a Phe173Leu substitution in the human G6PD protein. Since the 517 mutation does not create or remove any known restriction site, we introduced an artificially created site by adding a primer containing a mismatched base to the PCR reaction mixture. The mismatched base accompanying the nearby 517 T-->C mutation generates an XhoI site which is suitable for distinguishing normal from mutant alleles. Using this approach, the 517 mutation can be diagnosed quickly at the DNA level.

Fetal Blood↗
PubMed1976

[Characteristics of two new mutant forms of erythrocyte glucose-6-phosphate dehydrogenase: "Kirovograd" G6PD and "Zhitomir" G6PD].

The paper comprises the description of properties of three mutant forms of glucoso-6-phosphate dehydrogenase characterized according the WHO program. Preparations of the enzymes were isolated from erythrocytes of patients with G6PD deficiency from three unrelated to one another Ashkenasi families coming from the Ukraine and from Byelorussia. Two new variants of G6PD hitherto never described in the literature were discovered. These variants were designated as "Kirovograd" and "Zhitomir" after the towns the probands came from. The properties of purified enzymes revealed by the methods of the WHO program were as follows: the variant "Kirovograd" has a normal electrophoretic mobility in tris and TEB buffers and 98% of the normal in phosphate buffer. KM for G6P is 6,54; KM for NADP--2,19. It is characterized by a reduced thermostability and by an acute peak of activity at pH 8,5. The variant "Zhitomir" has 90-98% of the normal electrophoretic mobility in TEB buffer and 78-84% in phosphate buffer. KM for G6P is 5,4-8,3. KM for NADP is 1,4-3,1; with deoxyG6P is 50% and with deaminoNADP is 35%. It is also characterized with a reduced thermostability, while the curve of the dependence of its activity on pH has two peaks. Both variants are perfectly inactive with erythrocytes and thus should be assigned to the second group of the mutants variants of G6PD. The comparison of these variants to other variants encountered in the same national group revealed that they resemble certain quantitative variations.

Catalysis↗
PubMed1976

Mutant forms of erythrocyte glucose 6-phosphate dehydrogenase in Ashkenazi. Description of two new variants: G6PD Kirovograd and G6PD Zhitomir.

Two new variants of erythrocyte glucose 6-phosphate dehydrogenase are discovered in 3 unrelated Ashkenazi Jew patients with severe deficiency of enzyme. Both variants have a resemblance to 2 other variants in Ashkenazi: G6PD Boston and G6PD Kilgore, but have a significantly higher affinity for substrates and their analogues and are not associated with chronic hemolytic disease. Probably, all 4 variants arise from two ancestral mutations.

Genetic Variation↗
PubMed1989

Characterization of a new G6PD variant: G6PD Titusville.

We describe a new glucose-6-phosphate dehydrogenase mutant, G-6-PD Titusville. The propositus is a 7-month-old black male infant with a transient hemolytic episode. The mutant enzyme is characterized by abnormal electrophoretic mobility, thermolability, Km for NADP, abnormal deamino NADP use and a decreased sensitivity to inhibition by NADPH. G-6-PD activity of hemolysate, as measured under optimal in vitro conditions, was not initially decreased, whereas fibroblasts, granulocytes, and platelets showed a markedly decreased level of enzyme activity. These properties identify G6PD Titusville as a unique variant of this X-linked, housekeeping enzyme. We conclude that although the propositus with G6PD Titusville had a transient hemolytic episode, we cannot be certain whether this association was a causative one.

Enzyme Stability↗
PubMedDate not supplied

Preliminary experience with the differential pH technique for glucose-6-phosphate dehydrogenase (G6PD) measurement in whole blood: application to an area with high prevalence of thalassaemia and G6PD deficiency.

A new differential pH technique for glucose-6-phosphate dehydrogenase quantitative determination in whole blood has been evaluated. It is a rapid (90 s/analysis), reproducible (C.V. within-run 3.7%; between-run: 2.8%) and accurate method (in comparison with WHO method: r = 0.970). Reference intervals in non-deficient males were evaluated in 167 non-thalassaemics and in 60 beta-thal heterozygotes. The G6PD activity in beta-thalassaemia carriers is higher than in normals; this is particularly true if the activity is expressed in terms of U/g Hb. The phenotypic distribution measured in females is in agreement with that calculated by the Hardy-Weinberg law based on the incidence of the Gd(-) gene in males.

Adolescent↗