Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase

E. J. Wolvetang; R. J. Wanders; R. B. Schutgens; J. A. Berden; J. M. Tager

doi:https://doi.org/10.1016/0304-4165(90)90166-T

Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase

E. J. Wolvetang, R. J. Wanders, R. B. Schutgens, J. A. Berden, J. M. Tager

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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 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

Original language	English
Pages (from-to)	6-11
Journal	BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume	1035
Issue number	1
DOIs	https://doi.org/10.1016/0304-4165(90)90166-T
Publication status	Published - 1990

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https://doi.org/10.1016/0304-4165(90)90166-T

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@article{263f423f496a4774818b4681e75ddee3,

title = "Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase",

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 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",

author = "Wolvetang, {E. J.} and Wanders, {R. J.} and Schutgens, {R. B.} and Berden, {J. A.} and Tager, {J. M.}",

year = "1990",

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language = "English",

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TY - JOUR

T1 - Properties of the ATPase activity associated with peroxisome-enriched fractions from rat liver: comparison with mitochondrial F1F0-ATPase

AU - Wolvetang, E. J.

AU - Wanders, R. J.

AU - Schutgens, R. B.

AU - Berden, J. A.

AU - Tager, J. M.

PY - 1990

Y1 - 1990

N2 - 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

AB - 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

U2 - https://doi.org/10.1016/0304-4165(90)90166-T

DO - https://doi.org/10.1016/0304-4165(90)90166-T

M3 - Article

C2 - 2166576

SN - 0304-4165

VL - 1035

SP - 6

EP - 11

JO - BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

JF - BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

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