Emes, M.J.; Erismann, Karl Hans (1984). Purification and properties of glycollate oxidase from Lemna minor L. International journal of biochemistry & cell biology, 16(12), pp. 1373-1378. Elsevier 10.1016/0020-711X(84)90243-X
Full text not available from this repository.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.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) |
UniBE Contributor: |
Erismann, Karl Hans |
Subjects: |
500 Science > 580 Plants (Botany) |
ISSN: |
1357-2725 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Peter Alfred von Ballmoos-Haas |
Date Deposited: |
31 Jan 2018 10:45 |
Last Modified: |
05 Dec 2022 15:06 |
Publisher DOI: |
10.1016/0020-711X(84)90243-X |
URI: |
https://boris.unibe.ch/id/eprint/101915 |
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