Abstract
Microbodies of the algaMougeotia were isolated in a linear sucrose gradient. The organelles, which moved to the density 1.24 g cm−3, contained about 70% of the glycolate oxidase (EC 1.1.3.1) found in this alga. The enzyme oxidized glycolate, utilizing either oxygen or 2,6-dichlorophenolindophenol (DCPIP) as the electron acceptor. L-Lactate was an alternate substrate; almost no D-lactate was utilized. In the presence of O2, a Km of 415 μM was determined for glycolate, whereas the Km for L-lactate was about 5,000 μM. In the presence of DCPIP, lower concentrations of glycolate and L-lactate were sufficient to obtain the highest rates of enzyme activity.
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Abbreviations
- DCPIP:
-
2,6-dichlorophenolindophenol
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Stabenau, H., Säftel, W. A peroxisomal glycolate oxidase in the algaMougeotia . Planta 154, 165–167 (1982). https://doi.org/10.1007/BF00387911
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DOI: https://doi.org/10.1007/BF00387911