Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase.
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 beta-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.
Wolvetang
E J
EJ
Department of Pediatrics, Academic Medical Centre, Amsterdam, The Netherlands.
Wanders
R J
RJ
Schutgens
R B
RB
Berden
J A
JA
Tager
J M
JM
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002499:Centrifugation, Density Gradient; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D008099:Liver / Q000201:enzymology*; D008297:Male; D008830:Microbodies / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases