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Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase |
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| Authors: | Ernst J. Wolvetang Ronald J.A. Wanders Ruud B.H. Schutgens Jan A. Berden Joseph M. Tager |
| Affiliation: | 1. Department of Pediatric, Academic Medical Centre, University of Amsterdam, Academic Medical Centre, Amsterdam, The Netherlands;2. Department of Pediatric, E.C. Slater Institute for Biochemical Research, University of Amsterdam, Academic Medical Centre, Amsterdam, The Netherlands |
| Abstract: | Highly purified peroxisomal fractions from rat liver contain ATPase activity (18.8 ± 0.1 nmol/min per mg, n = 6). This activity is about 2% of that found in purified mitochondrial fractions. Measurement of marker enzyme activities and immunoblotting of the peroxisomal fraction with an antiserum raised against the β-subunit of mitochondrial ATPase indicates that the ATPase activity in the peroxisomal fractions can not be ascribed to contamination with mitochondria or other subcellular organelles. From the sensitivity of the ATPase present in the peroxisomal fraction towards a variety of ATPase inhibitors, we conclude that it displays both V-type and F-type features and is distinguishable from both the mitochondrial F1F0-ATPase and the lysosomal V-type ATPase. |
| Keywords: | Peroxisome ATPase Permeability DCCD NEM SDS-PAGE sodium dodecyl sulphate polyacrylamide gel electrophoresis |
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