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Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores.
Jpn J Microbiol. 1976 Aug; 20(4):281-6.JJ

Abstract

Glucose-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.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

10455

Citation

Tanahashi, T, et al. "Purification and Properties of Glucose-6-phosphate Dehydrogenase From Bacillus Subtilis Spores." Japanese Journal of Microbiology, vol. 20, no. 4, 1976, pp. 281-6.
Tanahashi T, Tochikubo K, Hachisuka Y. Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores. Jpn J Microbiol. 1976;20(4):281-6.
Tanahashi, T., Tochikubo, K., & Hachisuka, Y. (1976). Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores. Japanese Journal of Microbiology, 20(4), 281-6.
Tanahashi T, Tochikubo K, Hachisuka Y. Purification and Properties of Glucose-6-phosphate Dehydrogenase From Bacillus Subtilis Spores. Jpn J Microbiol. 1976;20(4):281-6. PubMed PMID: 10455.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores. AU - Tanahashi,T, AU - Tochikubo,K, AU - Hachisuka,Y, PY - 1976/8/1/pubmed PY - 1976/8/1/medline PY - 1976/8/1/entrez SP - 281 EP - 6 JF - Japanese journal of microbiology JO - Jpn. J. Microbiol. VL - 20 IS - 4 N2 - Glucose-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. SN - 0021-5139 UR - https://www.unboundmedicine.com/medline/citation/10455/Purification_and_properties_of_glucose_6_phosphate_dehydrogenase_from_Bacillus_subtilis_spores_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0021-5139&date=1976&volume=20&issue=4&spage=281 DB - PRIME DP - Unbound Medicine ER -