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PLASMA MEMBRANE ATPase OF RED BEET phosphatase acide dans les lutooides du latex d ' Hevea brasiliensis -
T. Hodges (1976)
ATPases Associated with Membranes of Plant Cells
- Publisher
- Oxford University Press
- Copyright
- Copyright © 2021 American Society of Plant Biologists
- ISSN
- 0032-0889
- eISSN
- 1532-2548
- DOI
- 10.1104/pp.71.2.350
- Publisher site
- See Article on Publisher Site
Abstract
Abstract A membrane fraction enriched with a magnesium-dependent, monovalent cation-stimulated ATPase was isolated from red beet (Beta vulgaris L.) storage roots by a combination of differential centrifugation, extraction with KI, and sucrose density gradient centrifugation. This fraction was distinct from endoplasmic reticulum, Golgi, mitochondrial, and possibly tonoplast membranes as determined from an analysis of marker enzymes. The ATPase activity associated with this fraction was further characterized and found to have a pH optimum of 6.5 in the presence of both Mg2+ and K+. The activity was substrate specific for ATP and had a temperature optimum near 40°C. Kinetics with Mg:ATP followed a simple Michaelis-Menten relationship. However the kinetics of K+-stimulation were complex and suggestive of negative cooperativity. When monovalent cations were present at 2.5 millimolarity, ATPase was stimulated in the sequence K+ > Rb+ > Na+ > Li+ but when the concentration was raised to 50 millimolarity, the sequence changed to K+ ≥ Na+ ≥ Rb+ > Li. The activity was not synergistically stimulated by combinations of Na+ and K+. The enzyme was insensitive to NaN3, oligomycin, ouabain, and sodium molybdate but sensitive to N,N′-dicyclohexylcarbodiimide, diethylstilbestrol, and sodium vanadate. Based on the similarity between the properties of this ATPase activity and those from other well characterized plant tissues, it has been concluded that this membrane fraction is enriched with plasma membrane vesicles. 1 This research was supported by the Natural Sciences and Engineering Research Council of Canada and the Department of Education of Quebec. This content is only available as a PDF. © 1983 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
Journal
Plant Physiology – Oxford University Press
Published: Feb 1, 1983