ISOLATION, PURIFICATION, AND KINETIC-PROPERTIES OF OXALATE OXIDASE (EC-1.2.3.4) FROM BEET SHOOTS

Authors
AZARASHVILI TS EVTODIENKO VY KUDZINA LY
Citation
Ts. Azarashvili et al., ISOLATION, PURIFICATION, AND KINETIC-PROPERTIES OF OXALATE OXIDASE (EC-1.2.3.4) FROM BEET SHOOTS, Russian journal of plant physiology, 43(2), 1996, pp. 169-173
Citations number
19
Categorie Soggetti
Plant Sciences
Journal title
Russian journal of plant physiology → ACNP
ISSN journal
10214437
Volume
43
Issue
2
Year of publication
1996
Pages
169 - 173
Database
ISI
SICI code
1021-4437(1996)43:2<169:IPAKOO>2.0.ZU;2-1
Abstract
Oxalate oxidase with a specific activity as high as 8 EU/mg protein wa s isolated from beet (Beta vulgaris L.) shoots. The main properties of the enzyme were characterized: K-M (3 x 10(-4) M), the maximum rate o f reaction (3.5 mu mol/(min mg protein)), and its activation energy (2 9.7 kJ/mol at pH 4.0). It is concluded that this enzyme can be used fo r oxalate determination in biological fluids.