Purification and properties of glycollate oxidase from Lemna minor L.
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1. Glycollate oxidase has been purified to apparent homogeneity from Lemna minor L. grown on medium containing 7mM NO−3.
2. The enzyme is a highly basic protein with a sub-unit molecular weight of 42,000 and a holoprotein molecular weight of 250,000.
3. The Lemna enzyme is a flavoprotein with a broad specificity for straight chain α-hydroxy acids, the preferred substrate being glycollate.
4. It is also competitively inhibited by oxalate and phenyllactate.
5. A comparison is drawn between the physical properties of glycollate oxidase from a number of higher plants and the degree of sub-unit aggregation in the resulting protomers.
2. The enzyme is a highly basic protein with a sub-unit molecular weight of 42,000 and a holoprotein molecular weight of 250,000.
3. The Lemna enzyme is a flavoprotein with a broad specificity for straight chain α-hydroxy acids, the preferred substrate being glycollate.
4. It is also competitively inhibited by oxalate and phenyllactate.
5. A comparison is drawn between the physical properties of glycollate oxidase from a number of higher plants and the degree of sub-unit aggregation in the resulting protomers.
Date of Publication
1984
Publication Type
Article
Subject(s)
Language(s)
en
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Series
International journal of biochemistry & cell biology
Publisher
Elsevier
ISSN
1357-2725
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metadata.only