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At least 1,027 records · Page 57Linked to original sources
PubMedDate not supplied

Glucose-6-phosphate dehydrogenase in vitro correlated with in vivo activity and reticulocytosis.

In vitro activity of erythrocyte glucose-6-phosphate dehydrogenase (G-6-PD) does not always correlate with in vivo hemolytic manifestations. Many of these non-correlations are reviewed and can now be explained on the basis of altered substrate affinity and/or altered inhibition by intracellular metabolites. These alterations are not detected by standard assay conditions. The influence of a young erythrocyte population upon in vitro G-6-PD activity was determined and the lower limit of expected values shown to be raised at least to the mean of an average age erythrocyte population.

Erythrocyte Aging↗
PubMed1988

[Biology of glucose-6-phosphate dehydrogenase deficiency].

G-6-PD deficiency is predominant in the entire history of haemolytic anemias secondary to enzyme deficiency, since its represents, by far, the most frequent erythro-enzymopathy; it is also the most studied and the best known from the clinical as well as biological standpoints. Because of the ethnic groups particularly affected, this deficiency is essentially, in France, an imported pathology, even if there are a few true european cases. The biological diagnosis of the deficient patient is simple and well codified, but the interpretation of numerous variants of the enzyme remains quite complex. The recent cloning of the gene should provide a decisive progress in understanding these various deficiencies.

Anemia, Hemolytic↗
PubMed1980

[Gd- allele distribution patterns in Azerbaijan. III. The identification of mutant forms of glucose-6-phosphate dehydrogenase].

In 28 families with G6PD deficiency living in 3 settlements of Shekii district of Azerbaijan 11 G6PD variants of II and III classes differing by kinetic properties were identified according WHO program. 9 of them are characterized with the same electrophoretic mobility. Comparison of G6PD spectra in two subpopulations and in a mixed group permits to make a conclusion about existence of common and rare G6PD alleles in examined population. They distribute by gene drift supported by natural selection. Among 7 samples of G6PD with normal and increased activity two new variants of IV class -- Nukha and Bash-Kungut -- were found.

Alleles↗
PubMed1977

[Biochemical characterization of a new variant of glucose-6-phosphate dehydrogenase (G-6-PD) deficiency with favism: G-6-PD Bielefeld (author's transl)].

A new variant of G-6-PD with favism has been detected in a German family. After partial purification the enzyme was biochemically characterized. It revealed normal electrophoretic mobility, normal thermostability and a flat pH-activity curve. The Km-value for G-6-P was reduced, whereas this value was normal for NADP. The substrate analogues 2-desoxy G-6-P, Gal-6-p and deamino-NADP were utilized to increased rates. The biochemical data were compatible with the benign clinical course.

Adult↗
PubMed2003

Glucose-6-phosphate dehydrogenase deficiency does not result from mutations in the promoter region of the G6PD gene.

In this study, we investigated whether glucose-6-phosphate dehydrogenase (G6PD) promoter mutations are responsible for G6PD deficiency. We analysed the G6PD proximal promoter and the 5' untranslated region (UTR) in 65 G6PD-deficient individuals, in which no mutations have been found in the G6PD gene coding sequences, using a nonradioactive polymerase chain reaction/single-strand conformation polymorphism (PCR/SSCP) analysis. We identified no sequence variations in the G6PD core promoter or in the 5' UTR of these G6PD-deficient individuals, which indicates that G6PD deficiency is not associated with promoter mutations in the G6PD locus.

DNA Mutational Analysis↗
PubMed1992

Glucose-6-phosphate dehydrogenase variants in Hawaii.

Sequence analysis has been performed on the DNA of 13 glucose-6-phosphate dehydrogenase (G6PD) deficient males from Hawaii, 6 of Filipino, 6 of Laotian, and 1 of Chinese extraction. Four different mutations were found: A-->T at cDNA nt 835, G-->A at nt 871, C-->T at nt 1360, and G-->A at nt 1388. The mutations at nt 835 and nt 1360 have not been described previously, and the latter, in particular, appears to be relatively common. The nt 1360 mutation changes the same codon as is altered in a previously described mutation, G6PD Andalus.

China↗
PubMed1985

[Patterns of Gd- allele distribution in Azerbaijan. IV. The incidence and polymorphism of erythrocytic glucose-6-phosphate dehydrogenase deficiency in the settlement of Kobi, Apsheron District].

The frequency and polymorphism of erythrocyte G6Pd deficiency were studied in schoolchildren of Koby settlement, Apsheron district (n = 469). The total frequency of Gd- alleles was 3.6%. Out of 10 hemizygotes found 9 had Gd- alleles of the III class and 1 had Gd- allele of the II class. The mutant enzyme was isolated from 10 ml venous blood samples and studied according to WHO program. Three different mutant forms of G6PD were found, neither of them having been earlier described. One of these alleles was common for the population studied (n = 6).

Alleles↗
PubMed1995

Role of hemolysis in neonatal jaundice associated with glucose-6 phosphate dehydrogenase deficiency.

End-tidal carbon monoxide was measured in 108 newborn infants who had been screened for glucose-6-phosphate dehydrogenase (G6PD) deficiency. The mean +/- SD end-tidal carbon monoxide did not differ significantly between the G6PD-deficient and the normal neonates, 2.1 +/- 0.6 microliters/L and 2.0 +/- 0.5 microliters/L, respectively, within 12 hours of birth and 1.9 +/- 1.4 microliters/L and 1.5 +/- 0.7 microliters/L, respectively, at 48 to 72 hours after birth. On the basis of these measurements, hemolysis is not a sufficient explanation for jaundice in G6PD-deficient newborn infants in the transitional period.

Bilirubin↗
PubMed1992

New glucose-6-phosphate dehydrogenase mutations from various ethnic groups.

Seven new mutations that produce glucose 6 phosphate dehydrogenase (G6PD) deficiency are described. Three are in variants that were biochemically characterized and described previously, while four were found in samples that had not been characterized biochemically. Several of the mutations affect the amino acids that are mutated in other G6PD variants. As had been noted previously, variants that are associated with nonspherocytic anemia are located either near the glucose 6 phosphate or the NADP binding sites. Variants more distant from these sites are not associated with chronic hemolysis.

Amino Acid Sequence↗
PubMedDate not supplied

Glutathione reductase in the red blood cells.

Glutathione reductase plays an important role in protecting hemoglobin, red cell enzymes, and biological cell membranes against oxidative damage by increasing the level of reduced glutathone (GSSGR) in the process of aerobic glycolysis. The enzyme deficiency may result in mild to moderately severe hemolytic anemia upon exposure to certain drugs or chemicals. However, hereditary deficiency of the enzyme is extremely rare. Recent studies on glutathione reductase in the red cell have shown more insight in the understanding of red cell metabolism and interactions with other enzymes, especially glucose-6-phosphate dehydrogenase (G-6-PD). Glutathione reducatase in serum may be a source of error in any clinical laboratory test in which an enzyme activity is determined indirectly by measuring the change in reduced nicotinamide-adenine dinucleotide (NADH) or reduced nicotinamide adenine dinucleotide phosphate (NADPH) absorbance. Glutathione reductase levels are reduced in banked blood when citrate-phosphate-dextrose (CPD) is used as a preservative. Reviewed is the role of glutathione reductase in the metabolism of the red cell and its clinical implication and usefulness.

Erythrocytes↗
PubMed1992

Rapid isolation of glucose-6-phosphate dehydrogenase from human erythrocytes by combined affinity and anion-exchange chromatography for biochemical characterization of variants.

A new method is presented for the purification of human glucose-6-phosphate dehydrogenase (G6PD) using affinity chromatography with 2'5'-ADP-Sepharose 4B followed by automated ion-exchange chromatography with DEAE 5PW. This rapid method allows a high recovery of enzyme activity from even a small amount of blood; the yield is about 90% after the first purification step and 70% at the end of the procedure. There is an excellent reproducibility of the kinetic parameters and optimal biochemical characterization of G6PD is achieved even for variants associated with severe enzyme deficiency (e.g. G6PD Mediterranean).

Chromatography, Affinity↗
PubMed1982

Human hair follicles may be used for population screening of heterozygotes of glucose-6-phosphate dehydrogenase deficiency.

The carrier status for glucose-6-phosphate dehydrogenase deficiency can still be detected with the use of hair follicles after a period up to 10-14 days after plucking, even under conditions of temperature and humidity that are encountered in tropical countries, where the disease is most common. Furthermore, it is shown that the hair colour or age of the donor has no influence on the enzyme activity. As a consequence, the hair follicle is indeed suitable for screening in rural areas since mailing to existing medical centres is possible.

Adult↗
PubMed1977

Glucose-6-phosphate dehydrogenase (G6PD) activity of human sperm.

Sperm from normal human donors and a G6PD-A- individual were examined for x-linked glucose-6-phosphate dehydrogenase activity and autosomally linked 6-phosphogluconate dehydrogenase activity. With the use of fluorescence microscopy, we divised a procedure to visualise in individual sperm cells the fluorescence of reduced coenzyme NADPH formed by each of the two enzymes in the presence of appropriate substrates. We found significant differences in the population distribution of sperm expressing each of the two activities, and the ratio of the two activities in sperm homogenate is very different from the one found in erythrocyte lysates. The possibility of haploid gene expression has been considered in interpreting these results.

Electrophoresis, Disc↗
PubMed1981

Gd(-) Muret and gd(-) Colomiers, two new variants of glucose-6-phosphate dehydrogenase associated with favism.

Two males subjects are described with hitherto undescribed glucose-6-phosphate dehydrogenase (G6PD) variants. The first is of French ancestry, the second of Sicilian extraction. Each subject suffered from acute hemolytic anemia following ingestion of broad beans (Vicia fava). In both cases the hemolytic crisis occurred in a late period of life (29 and 58 years). No previous hemolytic crisis was recorded. The electrophoretic and kinetic properties of the mutant enzymes examined after purification from the red cells allowed each to be distinguished from other G6PD variants reported until now. The first variant was named Gd(-) Muret, the other Gd(-) Colomiers.

Adult↗
PubMed1982

G6PD Varadero. A new variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia.

A glucose-6-phosphate dehydrogenase (G6PD) variant was studied in a mulatto patient with chronic nonspherocytic hemolytic anemia. This variant has reduced activity, increased thermolability, a reduced Michaelis constant for glucose-6-phosphate, slightly increased electrophoretic mobility, a biphasic pH activity profile, high 2-deoxyglucose-6-phosphate utilization, normal diamino nicotinamide adenine dinucleotide phosphate utilization and a peak of elution profile after G6PD B. The electrophoretic, kinetic, and chromatographic properties of this erythrocyte G6PD variant allow the conclusion that G6PD Varadero is probably a new variant.

Anemia, Hemolytic, Congenital↗
PubMed1982

Glucose-6-phosphate dehydrogenase deficiency: genetic heterogeneity in Sardinia.

Glucose-6-phosphate dehydrogenase (G6PD) was partially purified from red blood cells of 44 Sardinian males with severe enzymatic deficiency and the variants characterized chromatographically and biochemically to see if there is genetic heterogeneity of the enzyme in Southern Sardinia. Three different variants associated with severe G6PD deficiency were identified: the common G6PD Mediterranean variant; G6PD Sassari, recently described by Testa et al. (1980), and a new variant that we have designated G6PD Cagliari. Family studies were carried out to demonstrate that these variants are due to the presence of different alleles.

Chromatography, Ion Exchange↗
PubMedDate not supplied

Glucose-6-phosphate dehydrogenase deficiency in Kuwait, Syria, Egypt, Iran, Jordan and Lebanon.

A total of 3,501 male subjects from six Arab countries living in Kuwait were investigated for quantitative and phenotypic distribution of red cell glucose-6-phosphate dehydrogenase (G6PD). The ethnic origins of those investigated were Kuwait, Egypt, Iran, Syria, Lebanon and Jordan. The distribution of G6PD deficiency among the different ethnic groups varied widely, ranging from 1.00% for Egyptians to 11.55% for Iranians. The activity of the normal enzyme was remarkably similar, with values ranging from 6.1 +/- 0.8 to 6.5 +/- 1.1 IU/g Hb. A low frequency of the Gd(A) allele was found in two ethnic groups, Egyptians (0.019) and Iranians (0.014). Gd(A-) was present at the very low frequency of 0.006 in another two ethnic groups, Kuwaitis and Jordanians.

Adolescent↗
PubMed1981

The interference of leukocytes and platelets with measurement of clucose-6-phosphate dehydrogenase activity of erythrocytes with low activity variants of the enzyme.

Complete removal of leukocytes and platelets from whole blood showed that the glucose-6-phosphage dehydrogenase (G6PD) activity in "pure" erythrocytes from G6PD deficient hemizygous Sardinian subjects is consistently lower than reported in the literature. Thus, although non of 27 hemizygous subjects showed undetectable erythrocyte G6PD activity, their levels ranged between 0.0015 and 0.008 IU/g Hb, as compared with a mean value of 4.5 IU/g Hb in normal subjects. Most of the biochemical peoperties that were formerly ascribed to erythrocyte G6PD appear to be those of the enzyme from contaminating leukocytes and (or) platelets.

Antibodies↗