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. 1978 Aug;62(2):165–172. doi: 10.1104/pp.62.2.165

Purification and Characterization of a Cation-stimulated Adenosine Triphosphatase from Corn Roots 1

Michael J Benson 1, Carl L Tipton 1
PMCID: PMC1092083  PMID: 16660479

Abstract

A membrane-bound, monovalent cation-stimulated ATPase from Zea mays roots has been purified to a single band on sodium dodecyl sulfate gel electrophoresis. Microsomal preparations with K+ -stimulated ATPase activity were extracted with 1 m NaClO4, and the solubilized enzyme was purified by chromatography on columns of n-hexyl-Sepharose, DEAE-cellulose, and Sephadex G-100 Superfine. A 500-fold purification over the activity present in the microsomes was obtained. The K+ -stimulated activity shows positive cooperativity with increasing KCl concentrations. The purified enzyme shows K+ -stimulated activity with ATP, GTP, UTP, CTP, ADP, α + β-glycerophosphate, p-nitrophenyl phosphate, and pyrophosphate as substrates. Under most conditions ATP is the best substrate. Although dicyclohexyl carbodiimide and Ca2+ inhibit and alkylguanidines stimulate the K+ -ATPase while bound to microsomes, they have no effect on the purified enzyme.

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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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