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. 1992 Nov;174(21):6911–6917. doi: 10.1128/jb.174.21.6911-6917.1992

Isolation and characterization of the high-affinity K(+)-translocating ATPase from Rhodobacter sphaeroides.

T Abee 1, A Siebers 1, K Altendorf 1, W N Konings 1
PMCID: PMC207370  PMID: 1400242

Abstract

Cells of the purple nonsulfur bacterium Rhodobacter sphaeroides express a high-affinity K+ uptake system when grown in media with low K+ concentrations. A vanadate-sensitive, K(+)-stimulated and Mg(2+)-stimulated ATPase was purified from membranes of these cells by solubilization with decyl-beta-D-maltoside in the presence of Escherichia coli phospholipids followed by triazine-dye affinity chromatography. This primary transport system has a substrate specificity and an inhibitor sensitivity closely similar to those of the Kdp ATPase from E. coli and is composed of three subunits with molecular masses of 70.0, 43.5, and 23.5 kDa.

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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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