Glucose-6-phosphate Dehydrogenase from Agaricus bisporus: Purification and Properties
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چکیده
منابع مشابه
Purification and properties of Penicillium glucose 6-phosphate dehydrogenase.
1. Glucose 6-phosphate dehydrogenase was isolated and partially purified from a thermophilic fungus, Penicillium duponti, and a mesophilic fungus, Penicillium notatum. 2. The molecular weight of the P. duponti enzyme was found to be 120000+/-10000 by gelfiltration and sucrose-density-gradient-centrifugation techniques. No NADP(+)- or glucose 6-phosphate-induced change in molecular weight could ...
متن کاملPurification and properties of d-glucose-6-phosphate dehydrogenase.
n-Glucose-6-phosphate dehydrogenase (Zwischenferment) was discovered by Warburg and Christian in 1931 (1, 2). An active preparation was obtained then from horse erythrocytes and in 1932 from the Lebedev juice made from brewers’ yeast (3). Because of its extreme specificity, this enzyme has become an important analytical tool. Various preparations of it have been described, the first being those...
متن کاملProduction , Purification and Properties of Extracellular Laccase of Agaricus bisporus
Extracellular laccase (EC 1 .14.18.1) of the cultivated mushroom Agaricus bisporus was produced constitutively in defined or complex media. No enzyme induction was found after treatment with cycloheximide or with other potential inducers such as toluidine or xylidine. The enzyme was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography, gel filtration and affin...
متن کاملPurification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus.
Glucose 6-phosphate dehydrogenase (EC 1.1.1.49) was purified from Aspergillus aculeatus, a filamentous fungus previously isolated from infected tongue of a patient. The enzyme, apparently homogeneous, had a specific activity of 220 units mg(-1), a molecular weight of 105,000 +/- 5,000 Dal by gel filtration and subunit size of 52,000 +/- 1,100 Dal by sodium dodecyl sulphate-polyacrylamide gel el...
متن کاملPurification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes.
Glucose 6-phosphate dehydrogenase (G6PD) was purified from turkey erythrocytes by ammonium sulphate precipitation and followed by ADP Sepharose affinity gel chromatography. The yield was 49.71% and specific activity of the enzyme was found to be 44.16 EU/mg protein. By gel filtration the molecular mass was found to be 75 kDa. The enzyme had an optimum pH at 9.0, and optimum temperature at 50 de...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1985
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-131-2-321