Studies on Dehydroascorbic Acid Reductase in Escherichia Colik12

Takiguchi, Hisashi

doi:10.5925/jnsv1954.11.114

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1967

2021

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Cited by 4 publications

References 7 publications

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Glutathion-Dehydrogenase (EC 1.8.5.1) aus Weizenmehl. Reindarstellung und Eigenschaften

Boeck

Grosch

1976

Z Lebensm Unters Forch

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Glutathione: dehydroascorbic acid oxidoreductase (EC 1.8.5.1) has been purified to essential homogeneity by precipitation with (NH4)2SO4, and ion-exchange chromatography on CM-Sephadex and DEAE-cellulose. The molecular weight is 24200 Dalton as determined by SDS-PAG-electrophoresis. The amino acid composition was analysed. The esed. The enzyme ist specific for glutathione as H-donor and it reduces the L-threo-diasteromer faster than the L-erythro- and D-erythro-dehydroascorbic acid. The enzyme is inhibited by iode acetic acid and N-ethyl-maleinimide. Zero-order kinetics was only observed for the hydrogen-acceptor but not for glutathione.

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Glutathion-Dehydrogenase (EC 1.8.5.1) aus Weizenmehl. Reindarstellung und Eigenschaften

Boeck

Grosch

1976

Z Lebensm Unters Forch

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Verfahren zur Bestimmung der Aktivit�t der Glutathion-Dehydrogenase (EC 1.8.5.1). Vorkommen des Enzyms in verschiedenen Weizensorten

Kahnt

Mundy

Grosch

1975

Z Lebensm Unters Forch

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2,6-dichlorophenol-indophenol is more stable in 75% ethanol than in aqueous solution and ascorbic acid reacts considerably faster in this media than glutathione. The activity determination of glutathione: dehydroascorbic acid oxidoreductase was based on these observations by a photometric measurement of the ascorbic acid resulting from the catalysis. Extracts from various types of wheat were tested and relatively high enzyme activities were found.

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A ‘dehydroascorbic acid reductase’ factor in guinea-pig tissues

Grimble¹,

Hughes²

1967

Experientia

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Studies on Dehydroascorbic Acid Reductase in Escherichia Colik12

Cited by 4 publications

References 7 publications

Glutathion-Dehydrogenase (EC 1.8.5.1) aus Weizenmehl. Reindarstellung und Eigenschaften

Glutathion-Dehydrogenase (EC 1.8.5.1) aus Weizenmehl. Reindarstellung und Eigenschaften

Verfahren zur Bestimmung der Aktivit�t der Glutathion-Dehydrogenase (EC 1.8.5.1). Vorkommen des Enzyms in verschiedenen Weizensorten

A ‘dehydroascorbic acid reductase’ factor in guinea-pig tissues

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