Results 171 to 180 of about 17,774 (212)
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6-Phosphogluconate dehydrogenase deficiency in an Italian family
Annals of Hematology, 2001A rare case of hereditary erythrocyte enzymopathy, namely 6-phosphogluconate dehydrogenase (6PGD) deficiency, was found in an Italian family. The activity of the enzyme was reduced to 35% in the propositus and her mother, but was normal in the other three members of the family.
Caprari, P +7 more
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6-Phosphogluconate dehydrogenase in sea urchin embryos
Experimental Cell Research, 1963Abstract 6-Phosphogluconate dehydrogenase activity was studied in the developing sea urchin embryo. After fertilization the activity increased and two individual peaks of high activity were observed, one at the late cleavage stage and the other shortly after hatching. In later stages the enzyme activity varied at a lower level.
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Molecular Size Studies on 6-Phosphogluconate Dehydrogenase
Nature, 1966GENETICALLY determined electrophoretic variants of 6-phosphogluconate dehydrogenase (6-PGD) have been found in man and rat1, pigeon2, deer mouse3, and the fruit fly4. In all five species the heterozygous phenotype contains the two parental enzyme forms plus a third 6-PGD of intermediate electrophoretic mobility on starch gel.
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6-Phosphogluconate Dehydrogenase Gene: pgd
1993Abstract The sequence of Drosophila 6-PGD is 50% identical to prokaryotic 6-PGD and 60-70% identical to the porcine and ovine enzymes (Fig. 24.1) (Scott and Lucchesi 1991). 6-PGD is a homodimer; the monomer has a Mr of approximately 53 kD (Williamson et al. 1980).
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Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989Haemophilus influenzae 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating), EC 1.1.1.44) was purified 308-fold to electrophoretic homogeneity with a 16% recovery through a five-step procedure involving salt fractionation and hydrophobic and affinity chromatography.
H, Yoon, C D, Anderson, B M, Anderson
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Automated purification of human erythrocytic 6-phosphogluconate dehydrogenase
Journal of Chromatography A, 1982Human 6-phosphogluconate dehydrogenase (6PGD) was purified from hemolyzate by group affinity chromatography on 2',5'-ADP-Sepharose, followed by buffer exchange chromatography on Sephadex G-25 and finally salting-out chromatography on Sepharose 6B. An apparatus was assembled from commercially available elements, in which the purification procedure can ...
Y, Kroviarski +3 more
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A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei
Molecular and Biochemical Parasitology, 1993A Trypanosoma brucei gene encoding 6-phosphogluconate dehydrogenase (6-PGDH) (EC 1.1.1.44) was identified and cloned by functional complementation of Escherichia coli gnd mutants with genomic trypanosome DNA. The T. brucei gnd gene is present as a single copy.
M P, Barrett, R W, Le Page
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1963
Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
F H, BURNS, P H, WERNERS
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Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
F H, BURNS, P H, WERNERS
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6-Phosphogluconate dehydrogenase: Structural symmetry and functional asymmetry
Protein & Peptide Letters, 2000Abstract: 6-Phosphogluconate dehydrogenase catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate through an oxidation, a decarboxylation and a tautomerization. The two subunits in the crystals of the dimeric sheep liver enzyme have the same conformation, as the apoenzyme and with the substrate or coenzyme. An hypothesis
RIPPA, Mario +3 more
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Human granulocyte 6 phosphogluconate dehydrogenase
Biochimie, 1975Dominique Cottreau +4 more
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