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Differential binding of hnRNP K, L and A2/B1 to an exonic splicing silencer element located within exon 12 of glucose-6-phosphate dehydrogenase mRNAGriffith, Brian Nelson. January 2006 (has links)
Thesis (Ph. D.)--West Virginia University, 2006. / Title from document title page. Document formatted into pages; contains xi, 183 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Regulation of glucose-6-phosphate dehydrogenase by polyunsaturated fatty acids in cultured rat hepatocytesStabile, Laura P. January 1999 (has links)
Thesis (Ph. D.)--West Virginia University, 1999. / Title from document title page. Document formatted into pages; contains x, 125 p. : ill. Vita. Includes abstract. Includes bibliographical references.
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Signaling pathways involved in regulation of glucose-6-phosphate dehydrogenase (G6PD) by arachidonic acidTalukdar, Indrani. January 2006 (has links)
Thesis (Ph. D.)--West Virginia University, 2006. / Title from document title page. Document formatted into pages; contains viii, 123 p. : ill. (some col.). Includes abstract. Includes bibliographical references.
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The effect of nutrients upon the activity of SR proteinsWalsh, Callee McConnell. January 1900 (has links)
Thesis (Ph. D.)--West Virginia University, 2009. / Title from document title page. Document formatted into pages; contains vii, 91 p. : ill. (some col.). Includes abstract. Includes bibliographical references.
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The study of glucose-6-phosphate dehydrogenase (G6PD) gene regulation in HepG2 cells by glucose induction and the study of G6PD mRNA localization by fluorescent in situ hybridization (FISH)Griffith, Brian Nelson. January 2002 (has links)
Thesis (M.S.)--West Virginia University, 2002. / Title from document title page. Document formatted into pages; contains viii, 100 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references (p. 80-96).
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Estudo complementar da glicose-6-fosfato desidrogenase eritrocitária do marsupial brasileiro Didelphis marsupialis / Complementary study of glucose-6-phosphate dehydrogenase erythrocyte of brazilian marsupial Didelphis marsupialisPinto, Sheila Serra Vieira 18 February 2009 (has links)
Sabe-se que a atividade da glicose-6-fosfato desidrogenase eritrocitária do marsupial brasileiro Didelphis marsupialis é cerca de 15 a 20 vezes a encontrada nos eritrócitos humanos. Pretendendo-se investigar se esta hiperatividade também se encontra ou não aumentada nas outras enzimas eritrocitárias, levou-se a efeito a dosagem das atividades das enzimas glicolíticas bem de outras enzimas relacionadas ao metabolismo óxido-redutor do eritrócito do marsupial. Alguns dados bioquímicos sorológicos, hematológicos e imunológicos foram também obtidos. Assim sendo, as seguintes enzimas eritrocitárias foram estudadas: hexoquinase, glicose fosfato isomerase, fosfofrutoquinase, aldolase, triose fosfato isomerase, gliceraldeido-3-fosfato desidrogenase, fosfogliceratoquinase, difosfoglicerato mutase, monofosfoglicerato mutase, enolase, piruvato quinase, lactato desidrogenase, glicose-6-fosfato desidrogenase, 6-fosfogliconato desidrogenase, glutationa redutase, glutationa peroxidase, glutationa S-transferase, nicotinamida adenina dinucleotideo fosfato diaforase, nicotinamida adenina dinucleotideo meta-hemoglobina redutase, superóxido dismutase, aspartato aminotransferase, adenilato quinase, adenosina desaminase e acetilcolinesterase. Embora a maioria das enzimas estudadas tenham revelado atividades semelhantes às encontradas nos eritrócitos humanos, foram observados aumentos significativos da hexoquinase, piruvato quinase e glutationa S-transferase. Entretanto, a atividade da glutationa peroxidase apresentou grande aumento de atividade, cerca de dez a doze vezes a encontrada nos eritrócitos humanos, talvez agindo em conjunto com a hiperatividade da glicose-6-fosfato desidrogenase da ordem de dez a quinze vezes já descrita nos eritrócitos humanos / It is known that erythrocyte glucose-6-phosphate dehydrogenase specific activity of Didelphis marsupialis is about 15-20 times higher than human red cells. In order to investigate whether this hyperactivity is extended or not to other red cell enzymes, it was proposed to ascertain the activity of the glycolytic enzymes as well as other related to the redox metabolism of the opossum erythrocyte. Some biochemical, hematological and immunological data were also assayed as well. That being so, the following red cell enzymes were assayed: hexokinase, glucose phosphate isomerase, phosphofructokinase, aldolase, triose phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, diphosphoglycerate mutase, monophosphoglycerate mutase, enolase, pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glutathione reductase, glutathione peroxidase, glutathione S-transferase, nicotinamide adenine dinucleotide phosphate diaphorase, nicotinamide adenine dinucleotide metahemoglobin reductase, superoxide dismutase, aspartate amino-transferase, adenylate kinase, adenosine deaminase and acetylcholinesterase . Although most of the enzymatic activities disclosed to be similar to humans, some enzymes exhibited high activities as the hexokinase, pyruvate kinase and glutathione-S-transferase, about three to four times in relation to human. However the glutathione peroxidase presented overwhelming activity, at the order of ten-twelve times the human enzyme, perhaps working together the glucose-6-phosphate dehydrogenase hyperactivity at the order of ten-fifteen times already described in the marsupial erythrocytes
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The molecular mechanism of glucose-6-phosphate dehydrogenase regulation by dietary factors in intact animalsAmir-Ahmady, Batoul. January 2000 (has links)
Thesis (Ph. D.)--West Virginia University, 2000. / Title from document title page. Document formatted into pages; contains xi, 126 p. : ill. Vita. Includes abstract. Includes bibliographical references (p. 93-115).
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Estudo complementar da glicose-6-fosfato desidrogenase eritrocitária do marsupial brasileiro Didelphis marsupialis / Complementary study of glucose-6-phosphate dehydrogenase erythrocyte of brazilian marsupial Didelphis marsupialisSheila Serra Vieira Pinto 18 February 2009 (has links)
Sabe-se que a atividade da glicose-6-fosfato desidrogenase eritrocitária do marsupial brasileiro Didelphis marsupialis é cerca de 15 a 20 vezes a encontrada nos eritrócitos humanos. Pretendendo-se investigar se esta hiperatividade também se encontra ou não aumentada nas outras enzimas eritrocitárias, levou-se a efeito a dosagem das atividades das enzimas glicolíticas bem de outras enzimas relacionadas ao metabolismo óxido-redutor do eritrócito do marsupial. Alguns dados bioquímicos sorológicos, hematológicos e imunológicos foram também obtidos. Assim sendo, as seguintes enzimas eritrocitárias foram estudadas: hexoquinase, glicose fosfato isomerase, fosfofrutoquinase, aldolase, triose fosfato isomerase, gliceraldeido-3-fosfato desidrogenase, fosfogliceratoquinase, difosfoglicerato mutase, monofosfoglicerato mutase, enolase, piruvato quinase, lactato desidrogenase, glicose-6-fosfato desidrogenase, 6-fosfogliconato desidrogenase, glutationa redutase, glutationa peroxidase, glutationa S-transferase, nicotinamida adenina dinucleotideo fosfato diaforase, nicotinamida adenina dinucleotideo meta-hemoglobina redutase, superóxido dismutase, aspartato aminotransferase, adenilato quinase, adenosina desaminase e acetilcolinesterase. Embora a maioria das enzimas estudadas tenham revelado atividades semelhantes às encontradas nos eritrócitos humanos, foram observados aumentos significativos da hexoquinase, piruvato quinase e glutationa S-transferase. Entretanto, a atividade da glutationa peroxidase apresentou grande aumento de atividade, cerca de dez a doze vezes a encontrada nos eritrócitos humanos, talvez agindo em conjunto com a hiperatividade da glicose-6-fosfato desidrogenase da ordem de dez a quinze vezes já descrita nos eritrócitos humanos / It is known that erythrocyte glucose-6-phosphate dehydrogenase specific activity of Didelphis marsupialis is about 15-20 times higher than human red cells. In order to investigate whether this hyperactivity is extended or not to other red cell enzymes, it was proposed to ascertain the activity of the glycolytic enzymes as well as other related to the redox metabolism of the opossum erythrocyte. Some biochemical, hematological and immunological data were also assayed as well. That being so, the following red cell enzymes were assayed: hexokinase, glucose phosphate isomerase, phosphofructokinase, aldolase, triose phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, diphosphoglycerate mutase, monophosphoglycerate mutase, enolase, pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glutathione reductase, glutathione peroxidase, glutathione S-transferase, nicotinamide adenine dinucleotide phosphate diaphorase, nicotinamide adenine dinucleotide metahemoglobin reductase, superoxide dismutase, aspartate amino-transferase, adenylate kinase, adenosine deaminase and acetylcholinesterase . Although most of the enzymatic activities disclosed to be similar to humans, some enzymes exhibited high activities as the hexokinase, pyruvate kinase and glutathione-S-transferase, about three to four times in relation to human. However the glutathione peroxidase presented overwhelming activity, at the order of ten-twelve times the human enzyme, perhaps working together the glucose-6-phosphate dehydrogenase hyperactivity at the order of ten-fifteen times already described in the marsupial erythrocytes
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