| DOI | Resolve DOI: https://doi.org/10.1139/m71-019 |
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| Author | Search for: Oka, T.1; Search for: Simpson, F. J.1; Search for: Child, J. J.1; Search for: Mills, Sister Cecily1 |
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| Affiliation | - National Research Council of Canada. Prairie Regional Laboratory
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| Format | Text, Article |
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| Abstract | Evidence is presented that a single enzyme, quercetinase, is responsible for the degradation of quercetin by Aspergillus flavus to yield carbon monoxide and a depside, 2-protocatechuoylphloroglucinol carboxylic acid. A procedure for the isolation of the dioxygenase as a homogeneous protein is described. The most purified preparation degraded 10 800 μmoles of quercetin/h mg protein and was homogeneous as judged by ultracentrifugation and by electrophoresis. The molecular weight was determined as 111 000 + 4000. Kₘ values for quercetin and oxygen as substrates were 5.2 × 10⁻⁶ M and 1.2 × 10⁻⁴ M respectively. The enzyme is a glycoprotein containing 27.5% carbohydrate and the amino acid composition is presented. |
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| Publication date | 1971-01-01 |
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| Publisher | Canadian Science Publishing |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| Identifier | NRCC-11638 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 485846d8-d2f3-4934-b953-1d8179751a18 |
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| Record created | 2023-09-13 |
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| Record modified | 2023-09-13 |
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