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Results for “GLUCOSEPHOSPHATE DEHYDROGENASE”

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At least 1,009 records · Page 56Linked to original sources
PubMed1979

Glucose-6-phosphate dehydrogenase deficiency: biochemical and histochemical studies on hair roots for carrier detection.

Kinetic properties of human hair root glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were studied in order to optimize the assay of these enzymes in lysates from single hair roots. In contrast to previously reported methods, an excess of purified 6-phosphogluconate dehydrogenase was added to the glucose-6-phosphate dehydrogenase reaction mixtures, thus allowing a more exact quantification of glucose-6-phosphate dehydrogenase activity. Although enzyme histochemical techniques suggest a similar distribution of hair root glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, enzyme assays on hair root segments after microdissection nevertheless indicate differences in the distribution of these enzymes. Upon storage a gradual drop in the activity of both hair root enzymes was found, but the rate of decrease in enzyme activity was about equal: the enzyme activity ratio was, therefore, not affected. This opens interesting possibilities for mailing hair roots for screening purposes without any special precautions.

Genetic Carrier Screening↗
PubMed1978

[Electrophoretic and kinetic properties of erythrocyte glucose-6-phosphate dehydrogenase (Gd) in hereditary enzyme deficiency. A new variant of glucose-6-phosphate dehydrogenase : Gd Kremenchug].

A study of the activity of human erythrocyte G-6-PD has been completed on a great number of normal controls, coming from different regions of the USSR. This study has led to the discovery of a new variant of erythrocytic Gd, which was named "Kremenchug" from the origin of the patient. This new Gd, has a very low Km for G-6-P, and has a greater affinity for 2-deoxyglucose-6-phosphate. The maximal activity versus the pH of the medium is also characteristic of this new Gd.

Adult↗
PubMed1997

A comprehensive method to scan for point mutations of the glucose 6 phosphate dehydrogenase gene.

We have developed a fast and comprehensive method to scan for point mutations in a gene on X chromosome. A target region of the gene is first amplified. Then, using the amplified product as a template, PCR is carried out with multiple short-length forward primers arrayed in tandem in the scanned region, and a common reverse primer. The absence of amplified product defines the site of a mutation within a narrow region of the primer recognition site. To evaluate our method, point mutations in exon 12 of the human glucose-6-phosphate dehydrogenase (G6PD) gene were used as a model system. Out of 12 Singaporean G6PD-deficient patients, 6 cases were shown by the method to have a nucleotide change in this exon. Sequence analysis confirmed the presence of a nucleotide change in the region identified by our scanning. Thus, our method is accurate in localizing mutations within a narrow region, and allows large numbers of samples to be handled simultaneously.

Chromosomes, Human, X↗
PubMed2001

Antioxidant capacity of G-6-PD-deficient erythrocytes.

Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency is the most common human enzymopathy. In this research, we studied two groups consisting of 30 male subjects who are G-6-PD deficient and 30 normal male subjects matched with the G-6-PD-deficient patients for age. All 30 assays were performed under normal conditions free of any oxidative attack that may result in haemolytic crisis in G-6-PD-deficient subjects. The erythrocyte glucose-6-phosphate dehydrogenase, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione-S-transferase (GST) activities, reduced glutathione (GSH) levels and erythrocyte and plasma thiobarbituric acid-reactive substances (TBARS) levels were measured. All parameters in each group did not differ significantly except for G-6-PD levels. These data show that G-6-PD-deficient subjects can survive in normal conditions unless they are exposed to any oxidative stress.

Antioxidants↗
PubMed1975

The detection of glucose-6-phosphate dehydrogenase deficiency in mediterraneans by comparative quantitative enzyme electrophoresis.

Glucose-6-phosphate dehydrogenase (G6PD) can be easily isolated from haemolysates by cellulose acetate electrophoresis, and heterozygous (as well as hemizygous and homozygous) G6PD deficiency can be readily detected if the activity of the enzyme is determined densitometrically after electrophoresis and expressed as a ratio of the activity of a second enzyme, 6-phosphogluconate dehydrogenase (6PGD), which is isolated at the same time and whose activity is similarly determined. A method is presented here, together with the results of a recent survey in which 400 babies of Greek origin were tested for G6PD deficiency by the method. An overall incidence of 4-3% was found in the group; 2-9% of the males were completely G6PD deficient and 5-2% of the females were heterozygous for the deficiency.

Australia↗
PubMed1982

G6PD-Puerto Limón: a new deficient variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia.

A new glucose-6-phosphate dehydrogenase (G6PD) variant with total deficiency associated with congenital nonspherocytic hemolytic anemia was found in a Costa Rican family. The study of the partially purified enzyme revealed thermal instability, increased G6P affinity, abnormal pH optimum, increased utilization of analogues, and a chromatographic behavior that differs from all the variants previously described. Thus, this new variant was designated G6PD Puerto Limón.

Adult↗
PubMed1979

Characterization of some erythrocyte G6PD variants by isoelectric focusing.

The existence of a microheterogeneity of glucose-6-phosphate dehydrogenase (G6PD) in human erythrocyte lysates has been previously demonstrated using isoelectric focusing (Der Kaloustian et al., 1974; Turner et al., 1975). The application of this method, modified in some aspects, to the identification of various G6PD variants led to interesting conclusions. The results reported here have been obtained from a study of four distinct molecular types: Gd(-) Mediterranean, Gd(-) Kabyle, the African Gd(+) A, and a new almost undescribed G6PD variant with severe enzyme deficiency named Gd(-) Muret.

Adolescent↗
PubMed2005

Red cell enzymes.

Mutations leading to red cell enzyme deficiencies can be associated with diverse phenotypes that range from hemolytic anemia, methemoglobinemia, polycythemia, and neurological and developmental abnormalities. While most of these mutations occur sporadically, some such as common glucose-6-phosphate dehydrogenase (G6PD) mutants are endemic and rarely cause disease. Common G6PD mutants likely reached their prevalence because they provide some protection against severe malarial complications. In this review G6PD, pyruvate kinase, 5' nucleotidase, and cytochrome b5 reductase deficiencies will be discussed in greater detail. Limitations of commonly used screening tests for detection of these disorders will also be emphasized, as well as emerging knowledge about non-enzymatic function of the glycolytic enzymes.

5'-Nucleotidase↗
PubMed1980

G6PD (Dublin): chronic non-spherocytic haemolytic anaemia resulting from glucose-6-phosphate dehydrogenase deficiency in an Irish kindred.

A new variant of G6PD associated with chronic non-spherocytic haemolytic anaemia (CNSHA) in an Irish male is described. This variant is unique in that it has a normal electrophoretic mobility, Michaelis constant for G6P and NADP, and a normal pH optimum, together with a marked increase in utilisation of the substrate 2 deoxy glucose-6-phosphate. It is also relatively heat stable when compared with the normal (B) variant. These characteristics distinguish this variant from previously reported variants associated with CNSHA and we have called it G6PD Dublin.

Adult↗
PubMed1979

[Study of the electrophoretic and kinetic properties of erythrocyte glucose-6-phosphate dehydrogenase in hereditary enzyme deficiencies. Description of a new variant of glucose-6-phosphate dehydrogenase: the Gd Kremenchug].

A study of the activity of human erythrocyte G-6-PD has been completed on a great number of normal controls, coming from different regions of the USSR. This study has led to the discovery of a new variant of erythrocytic Gd, which was named "Kremenchug" from the origin of the patient. This new Gd, has a very low Km for G-6-P, and has a greater affinity for 2-deoxyglucose-6-phosphate. The maximal activity versus the pH of the medium is also characteristic of this new Gd.

Adult↗
PubMed1984

The effect of in vivo ozone exposure to Dorset sheep, an animal model with low levels of erythrocyte glucose-6-phosphate dehydrogenase activity.

Female Dorset sheep were exposed in vivo to ambient ozone levels of 0.12 ppm, 0.25 ppm, 0.50 ppm, 0.70 ppm for 2.75 hours and the effects of this exposure upon erythrocytes were studied. Ozone exposure induced biochemical evidence of oxidant stress as indicated by decreases in GSH levels (at 0.5 and 0.7 ppm ozone) and ACHE (at 0.7 ppm), increases in MetHb (from 0.12 ppm upward) and decreases in red blood cell counts (from 0.12 ppm upward). However, only the decrease in GSH levels at the 0.5 ppm ozone exposure was statistically significant (p = 0.05).

Acetylcholinesterase↗
PubMed1976

Isolation of mammalian cell mutants deficient in glucose 6-phosphate dehydrogenase by means of a replica-plating technique.

A replica-plating technique is described which was used for the isolation of G-6-PD-deficient mutants in cultures of mutagen-treated Chinese hamster cells. Mutants were recognized by their failure to stain in a histochemical G-6-PD-specific staining reaction. Four mutants were isolated and characterized by growth properties, stability of their variant phenotypes, and reduced G-6-PD activity. One of these mutants on electrophoresis exhibited a variant G-6-PD and thus is very likely the result of a mutation in the structural gene for G-6-PD.

Animals↗
PubMed1978

A variant glucose-6-phosphate dehydrogenase Gd(-) Chiapas associated with moderate enzyme deficiency and occasional hemolytic anemia.

Erythrocyte glucose-6-phosphate deficiency is an X-chromosomal-linked hereditary trait often associated with hemolytic anemia. This report defines a new variant designated as Gd(-) Chiapas, which was found in a subject with occasional hemolytic jaundice. The red cell enzyme activity of the subject is about 15% of normal. The variant enzyme is thermolabile in vitro and has faster-than-normal anodal electrophoretic mobility and stronger-than-normal substrate affinity. The patient's hemolytic problem might be correlated with instability of the variant enzyme under physiologic stress.

Adult↗
PubMed1975

[Description of new mutant forms of erythrocyte glucose-6-phosphate dehydrogenase in man].

9 variants of human erythrocyte glucose-6-phosphate dehydrogenase (G6PD) were isolated from erythrocytes of patients with G6PD deficiency and partially purified according to WHO program for stanartization of methods for studying G6PD. The results of physico-chemical study of these enzymes (determination of electrophoretic mobility, kappaM for G6P and NADP, pH optimum and thermostability) permit tu consider 5 of them to be new mutations of G6PD previously not described in literature. The observed high geterogeneity of variants of G6PD in Azerbaijan is discussed.

Azerbaijan↗
PubMed1993

Stable hybrid myotubes: a new model for studying re-expression of enzymatic activities in vitro.

Heterokaryons represent a stable and reproducible model system for the study of biochemical and molecular aspects responsible for muscle gene activation. Previous experiments have used this fusion system to demonstrate human gene activation in hybrids formed between human and non-human cells. The aim of this research was to apply this experimental model to the correction of a cytoplasmic activity, namely glucose-6-phosphate dehydrogenase (G6PD), in vitro, in hybrid myotubes formed between G6PD-negative and positive myoblasts. Different identification methods were used (Hoechst stain and Fluorescent Latex Microspheres, FLMs) to identify hybrid myotubes formed. We demonstrated the restoration of G6PD activity in all hybrid myotubes formed; we then tried to elucidate the mechanisms underlying the restoration of this specific activity and apply the results obtained to the understanding of more complex mechanisms involved in muscle gene activation.

Animals↗
PubMed2000

Transient inhibition of glucose utilization by erythrocytes during the acute stage of typhoid fever.

The exact reason for hemolysis of glucose-6-phosphate dehydrogenase-deficient (G6PD) erythrocytes in patients with typhoid fever is unknown. Therefore, glucose utilization by normal and G6PD-deficient erythrocytes was measured during incubation with plasma of healthy controls as well as from patients in acute or recovery stages of typhoid fever. Glucose utilization in normal and G6PD-deficient erythrocytes significantly decreased compared to the controls when incubated with plasma of patients with acute typhoid fever, which normalized to the baseline after recovery from typhoid fever, suggesting an acquired alteration in G6PD enzyme properties by Salmonella typhi or its endotoxins.

Erythrocytes↗