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Biomedical subjects

Y Hachisuka

Publications and source records attributed to Y Hachisuka.

At least 37 records · Page 2Linked to original sources
PubMed1976

Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores.

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.

Bacillus subtilis↗
PubMed1974

L-amino acid dehydrogenases in Bacillus subtilis spores.

The presence of two kinds of l-amino acid dehydrogenase in resting spores of Bacillus subtilis was indicated. One of them was l-alanine dehydrogenase, which used only l-alanine as a substrate, and the other was nonspecific dehydrogenase, which used l-valine, l-isoleucine, l-leucine, and l-alanine (slightly) as substrates. Several properties of these dehydrogenases were compared.

Alanine↗
PubMed1971

Reactivative action of ethylenediaminetetraacetic acid or dipicolinic acid on inactive glucose dehydrogenase obtained from heated spores of Bacillus subtilis.

Partially purified inactive glucose dehydrogenase obtained from spores which were heated at 87 or 90 C for 30 min is converted to an active from by the addition of ethylenediaminetetraacetic acid, dipicolinic acid, or some salts. The molecular weight of the inactive glucose dehydrogenase in the heated spores is about one-half of that of the active glucose dehydrogenase in the intact resting spores. The possibility is discussed that the active glucose dehydrogenase in the intact resting spores divides into subunits and is converted to stable and inactive form during heating of spores at a particular range of temperature (87 to 90 C).

Alcohol Oxidoreductases↗