 BackResearch Article ScienceAsia 13 (1987): 169-177 |doi: 10.2306/scienceasia1513-1874.1987.13.169
PURIFICATION AND CHARACTERIZATION OF OXALATE OXIDASE FROM SPINY PIGWEED
S. MONGKOLISIRIKIEAT AND C. SRISUWANABSTRACT: Oxalate oxidase activities were determined in various tissues of the spiny pigweed (Amarantus spinosus L.). The highest acivity was found in the leaves. Partial purification
of this enzyme from the leaves of spiny pigweed was accomplished by heat treatment,
ammonium suIfate fractionation, high speed centrifugation and DEAE-Sephacel chromatography. The enzyme was shown to be heat stable and to exhibit substrate specificity towards oxalic acid with a Km of 2.1 x 105M. The optimal pH was 4.5 and the optimal temperature was about 35-50 oC. The molecular weight as determined on a Sepharose 6B column was 265,000. The enzyme was moderately inhibited by azide and strongly
inhibited by fluoride and 2 Department of Biochemistry, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailand. Received 25 March 1987
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-mercaptoethanol. The high specific activity and recovery of oxalate oxidase obtained from spiny pigweed suggests that spiny pigweed is a good source
for preparation of this enzyme.
