Small 1985 Biochem J: Difference between revisions
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|year=1985 | |year=1985 | ||
|journal=Biochem J | |journal=Biochem J | ||
|abstract=A simple spectrophotometric assay was developed for peroxisomal fatty acyl-CoA oxidase activity. The assay, based on the | |abstract=A simple spectrophotometric assay was developed for peroxisomal fatty [[acyl-CoA oxidase]] activity. The assay, based on the H<sub>2</sub>O<sub>2</sub>-dependent oxidation of leuco-dichlorofluorescein catalysed by exogenous [[peroxidase]], is more sensitive than methods previously described. By using mouse liver samples, cofactor requirements were assessed and a linear relationship was demonstrated between dye oxidation and enzyme concentration. By using this assay on subcellular fractions, palmitoyl-CoA oxidase activity was localized for the first time in microperoxisomes of rat intestine. The assay was also adapted to measure D-amino acid oxidase activity, demonstrating the versatility of this method for measuring activity of other H<sub>2</sub>O<sub>2</sub>-producing oxidases. | ||
|editor=[[Gnaiger E]], | |editor=[[Gnaiger E]], | ||
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|preparations=Oxidase;biochemical oxidation | |preparations=Oxidase;biochemical oxidation | ||
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::::* Aminotriazole was used to prevent the destruction of | ::::* Aminotriazole was used to prevent the destruction of H<sub>2</sub>0<sub>2</sub> by endogenous [[catalase]]. |
Latest revision as of 18:34, 25 February 2018
Small GM, Burdett K, Connock MJ (1985) A sensitive spectrophotometric assay for peroxisomal acyl-CoA oxidase. Biochem J 227:205-10. |
Small GM, Burdett K, Connock MJ (1985) Biochem J
Abstract: A simple spectrophotometric assay was developed for peroxisomal fatty acyl-CoA oxidase activity. The assay, based on the H2O2-dependent oxidation of leuco-dichlorofluorescein catalysed by exogenous peroxidase, is more sensitive than methods previously described. By using mouse liver samples, cofactor requirements were assessed and a linear relationship was demonstrated between dye oxidation and enzyme concentration. By using this assay on subcellular fractions, palmitoyl-CoA oxidase activity was localized for the first time in microperoxisomes of rat intestine. The assay was also adapted to measure D-amino acid oxidase activity, demonstrating the versatility of this method for measuring activity of other H2O2-producing oxidases.
โข Bioblast editor: Gnaiger E
Labels: MiParea: Instruments;methods
Preparation: Oxidase;biochemical oxidation
- Aminotriazole was used to prevent the destruction of H202 by endogenous catalase.