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pubmed-article:10455pubmed:abstractTextGlucose-6-phosphate dehydrogenase [D-glucose-6-phosphate: NADP oxidoreductase, EC. 1. 1. 1. 49] obtained from spores of Bacillus subtilis PCI 219 strain was partially purified by filtration on Sephadex G-200, ammonium sulfate fractionation and chromatography on DEAE-Sephadex A-25 (about 54-fold). The optimum pH for stability of this enzyme was about 6.3 and the optimum pH for the reaction about 8.3. The apparent Km values of the enzyme were 5.7 X 10(-4) M for glucose-6-phosphate and 2.4 X 10(-4) M for nicotinamide adenine dinucleotide phosphate (NADP). The isoelectric point was about pH 3.9. The enzyme activity was unaffected by the addition of Mg++ or Ca++. The inactive glucose-6-phosphate dehydrogenase obtained from the spores heated at 85 C for 30 min was not reactivated by the addition of ethylenediaminetetraacetic acid, dipicolinic acid or some salts unlike inactive glucose dehydrogenase.lld:pubmed
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pubmed-article:10455pubmed:pagination281-6lld:pubmed
pubmed-article:10455pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:10455pubmed:year1976lld:pubmed
pubmed-article:10455pubmed:articleTitlePurification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores.lld:pubmed
pubmed-article:10455pubmed:publicationTypeJournal Articlelld:pubmed