Purification and Properties of α-Hydroxyglutarate Dehydrogenase of Peptococcus aerogenes

α-Hydroxyglutarate dehydrogenase (NAD + specific) of Peptococcus aerogenes was purified by manganese chloride treatment, ammonium sulfate fractionation and chromatographies with DEAE-cellulose, hydroxyapatite and' Sephadex G-200, and then crystallized in a colorless thin plate form by the addit...

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Published inAgricultural and biological chemistry Vol. 48; no. 7; pp. 1713 - 1719
Main Authors Otawara, Shigeki, Ohshima, Toshihisa, Esaki, Nobuyoshi, Soda, Kenji
Format Journal Article
LanguageEnglish
Published Tokyo Taylor & Francis 01.07.1984
Agricultural Chemical Society of Japan
Subjects
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Oxidoreductases
Purification
Enzyme
Peptococcus aerogenes
Bacteria
Technique
Peptococcaceae
Physicochemical properties
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Summary:α-Hydroxyglutarate dehydrogenase (NAD + specific) of Peptococcus aerogenes was purified by manganese chloride treatment, ammonium sulfate fractionation and chromatographies with DEAE-cellulose, hydroxyapatite and' Sephadex G-200, and then crystallized in a colorless thin plate form by the addition of ammonium sulfate. The enzyme has a molecular weight of approximately 53,000 and consists of two subunits identical in molecular weight (about 32,000). The isoelectric point of the enzyme is pH 3.7 ± 0.1. The enzyme acts almost exclusively on α-ketoglutarate and α-hydroxyglutarate. The Michaelis constants for α-ketoglutarate, NADH, α-hydroxyglutarate and NAD + are 0.12, 0.028, 0.67 and 0.077 mm, respectively.
ISSN:0002-1369
DOI:10.1080/00021369.1984.10866394