Purification and properties of glycollate oxidase from Lemna minor L.

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

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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.

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:

31 Jan 2018 10:45

Publisher DOI:

10.1016/0020-711X(84)90243-X

URI:

https://boris.unibe.ch/id/eprint/101915

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