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. 1986 Aug;81(4):1080–1085. doi: 10.1104/pp.81.4.1080

Purification and Properties of the H+-Translocating ATPase from the Plasma Membrane of Tomato Roots 1

Gordon E Anthon 1, Roger M Spanswick 1
PMCID: PMC1075489  PMID: 16664947

Abstract

The proton-translocating, plasma membrane ATPase was purified from tomato roots. At the final stage of purification approximately 80% of the protein was found in a single band with an apparent molecular weight of 90 kilodaltons. Cross-linking studies indicated that the ATPase normally exists as a trimer of catalytic subunits. No evidence was found for any additional subunits. The pH optimum for ATP hydrolysis by the purified protein was 6.5. Activity was stimulated by K+, especially at low pH, and inhibited by vanadate, N,N′-dicyclohexylcarbodiimide, and diethylstilbestrol; nitrate was weakly inhibitory. Activity was stimulated by lysolecithin but inhibited by sonicated phospholipids. The inhibition by lipids could be prevented if octylglucoside was added with the lipids; the combination of octylglucoside and lipids actually stimulated activity. The purified protein could be reconstituted into liposomes and catalyzed ATP-dependent, vanadate-sensitive proton translocation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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