A Proton Translocating ATPase Is Associated with the Peroxisomal Membrane of Yeasts View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

A. C. Douma , M. Veenhuis , W. Harder

ABSTRACT

The presence of an ATPase on the delimiting membrane of peroxisomes, present in methanol-grown cells of the yeastHansenula polymorphawas investigated. Biochemically an ATPase activity was associated with purified peroxisomes. The activity of this enzyme was also demonstrated cytochemically. After incubations with CeCl3 and ATP specific reaction products were localized on the outer layer of the peroxisomal membrane. The properties of the peroxisomal ATPase closely resembled those of the mitochondrial enzyme. However, they differed in the apparent Km for ATP which was 4-6 mM for the peroxisomal ATPase and 0.6–0.9 mM for the mitochondrial enzyme. In fluorescence quenching experiments the ATP—dependent generation of a pH-gradient across the membrane of isolated peroxisomes was demonstrated - rendering the peroxisomes internally acid — indicating the proton translocating nature of the peroxisomal ATPase. Peroxisomes present in intact cells of methanol-grown H. polymorpha are internally acid as was indicated by 31p nuclear magnetic resonance studies. By this method their internal pH was estimated to be 5.8–6.0, whereas the cytosolic pH was 7.1. Similar results, both by cytochemical and by NMR methods, were obtained with cells of Candida utilis and Trichosporon cutaneum X4, grown under conditions of extensive microbody proliferation. More... »

PAGES

199-204

Book

TITLE

Peroxisomes in Biology and Medicine

ISBN

978-3-642-71327-9
978-3-642-71325-5

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-71325-5_19

DOI

http://dx.doi.org/10.1007/978-3-642-71325-5_19

DIMENSIONS

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