Identity of aliphatic L- -hydroxyacid oxidase and glycolate oxidase from rat livers |
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Authors: | Y Ushijima |
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Institution: | Department of Biochemistry, School of Medicine, Gunma University, Maebashi, Gunma, Japan |
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Abstract: | l-α-Hydroxyacid oxidase and glycolate oxidase have been partially purified from rat livers and found to be identical, judging by substrate specificities, Km values for certain substrates and coenzyme (FMN), activation energy, inhibition rates by various reagents and pH optimum. Km values are as follows; glycolate, 2.4 × 10?4m; l-α-hydroxyisocaproate, 1.26 × 10?3; glyoxylate, 1.41 × 10?4m; and FMN, 1.13 × 10?6m. Km values for glycolate and FMN are one-tenth and one-twentieth the literature values for hepatic glycolate oxidase. Sucrose density gradient centrifugation establishes that this enzyme is located in hepatic peroxisomes. |
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