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- Title
Properties of Plasmamembrane ATPase and Mitochondrial ATPase of Saccharomyces cerevisiae.
- Authors
PETERS, P. H. J.; BORST-PAUWELS, G. W. F. H.
- Abstract
The properties of mitochondrial ATPase and plasmamembrane ATPase of Saccharomyces cerevisiae are compared. The pH dependence differs considerably. At low pH plasmamembrane ATPase is inactivated. High salt concentrations protect the ATPase against acid inactivation. K+ is more effective than Na+. The sensitivity of mitochondrial ATPase towards azide, Dio 9 and oligomycin is far greater than found with plasmamembrane ATPase. There are no indications that the membrane ATPase is involved directly either in monovalent cation uptake or in divalent cation uptake. Sr2+ and Ca2+ do not activate plasmamembrane ATPase and inhibit Mg2+‐activated ATPase. The substrate specificity of plasmamembrane ATPase is much greater than the substrate specificity of mitochondrial ATPase.
- Subjects
SACCHAROMYCES cerevisiae; BIOLOGICAL membranes; SACCHAROMYCES; SACCHAROMYCETACEAE; ENDOMYCETALES; HEMIASCOMYCETES
- Publication
Physiologia Plantarum, 1979, Vol 46, Issue 4, p330
- ISSN
0031-9317
- Publication type
Article
- DOI
10.1111/j.1399-3054.1979.tb02629.x