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A novel point mutation in a class IV glucose-6-phosphate dehydrogenase variant (G6PD São Paulo) and polymorphic G6PD variants in São Paulo State, Brazil Genet. Mol. Biol.
Oliveira,Raimundo Antonio G.; Oshiro,Marilena; Hirata,Mario H.; Hirata,Rosario D.C.; Ribeiro,Georgina S.; Medeiros,Tereza M.D.; Barretto,Orlando C. de O..
In this study, we used red cell glucose-6-phosphate dehydrogenase (G6PD) activity to screen for G6PD-deficient individuals in 373 unrelated asymptomatic adult men who were working with insecticides (organophosphorus and carbamate) in dengue prevention programs in 27 cities in São Paulo State, Brazil. Twenty-one unrelated male children suspected of having erythroenzymopathy who were attended at hospitals in São Paulo city were also studied. Fifteen of the 373 adults and 12 of the 21 children were G6PD deficient. G6PD gene mutations were investigated in these G6PD-deficient individuals by using PCR-RFLP, PCR-SSCP analysis and DNA sequencing. Twelve G6PD A-202A/376G and two G6PD Seattle844C, as well as a new variant identified as G6PD São Paulo, were detected...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucose-6-phosphate dehydrogenase; Mutations; Polymorphism; Variants.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572009000200007
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Erythrocyte glucose-6-phosphate dehydrogenase activity assay and affinity for its substrate under "physiological" conditions BJMBR
Leite,A.A.; Barretto,O.C. de O..
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...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Glucose-6-phosphate dehydrogenase; Red blood cells; G6PD activity and affinity.
Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001200004
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Partial purification of glucose-6-phosphate dehydrogenase by aqueous two-phase poly(ethyleneglycol)/phosphate systems BJM
Ribeiro,Marcela Zanella; Silva,Daniel Pereira; Vitolo,Michele; Roberto,Inês Conceição; Pessoa-Jr,Adalberto.
Glucose-6-phosphate dehydrogenase (G6PDH) is an important enzyme used in biochemical and medical studies and in several analytical methods that have industrial and commercial application. This work evaluated the extraction of G6PDH in aqueous two-phase system (ATPS) of poly(ethyleneglycol) (PEG)/phosphate buffer, using as enzyme source a medium prepared through commercial baker's yeast disruption. Firstly, the effects of PEG molar mass on the enzyme partition and of homogenization and rest on the system equilibrium were investigated. Afterwards, several ATPS were prepared using statistical analysis (2² factorial design). The results, including kinetic and thermodynamic parameters for the G6PDH activity, showed partial purification of this enzyme in ATPS...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aqueous two-phase systems; Glucose-6-phosphate dehydrogenase; Liquid-liquid extraction; Saccharomyces cerevisiae.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822007000100016
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The impacts of Elaeagnus umbellata Thunb. leaf and fruit aqueous extracts on mice hepatic, extrahepatic antioxidant and drug metabolizing enzymes related structures BJPS
Ozen,Tevfik; Yildirim,Kemal; Toka,Mehmet.
ABSTRACT In this work, the potential chemopreventive activities of Elaeagnus umbellata fruit aqueous (EUFA) and leaf aqueous (EULA) extracts focusing on the modulatory influence of xenobiotic metabolizing enzymes (XMEs), antioxidant enzymes, glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), lactate dehydrogenase (LDH) activity, lipid peroxidation (LP), sulfhydryl groups were investigated in the hepatic and extrahepatic organs of Swiss albino mice (50 and 100 mg/kg body wt given orally for 14 days) and compared with BHA (0.75 % in diet). The modulatory and chemopreventive properties of two different doses EUFA and EULA were observed for cytochrome P450, cytochrome b5, sulfhydryl groups, NADPH-cytochrome P450 reductase,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Elaeagnus umbellata Thunb; Chemopreventive properties; Xenobiotic metabolizing enzymes; Antioxidant enzymes; Lipid peroxidation; Glutathione; Lactate dehydrogenase; Glucose-6-phosphate dehydrogenase; 6-Phosphogluconate dehydrogenase..
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502017000300625
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Enzymatic activity in braúna seeds subjected to thermal stress Ciência Rural
Ataíde,Glauciana da Mata; Borges,Eduardo Euclydes de Lima e; Flores,Andressa Vasconcelos.
ABSTRACT: To occur seed germination distinct hydrolytic enzymes work together, enabling primary root protrusion. The objective of this study was to investigate changes in the activities of α-amylase, β-amylase, and glucose-6-phosphate dehydrogenase (G6PdH) during germination of Melanoxylon brauna Schott. seeds under thermal stress. To this end, seeds of this species were germinated under constant temperature (10, 25, 30 or 40°C) and samples were collected every 24h during a 96-h period, in which the activity of the enzymes were evaluated. At 25 and 30°C, optimal temperatures for the germination of the species, the activities of α-amylase, β-amylase, and G6PdH increased with seed imbibitions. At 10 and 40°C, enzyme activities decreased, impairing the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Α-amylase; Β-amylase; Glucose-6-phosphate dehydrogenase; Melanoxylon brauna.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782016000601044
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