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The KDP ATPase of Escherichia coli.
Altendorf K, Siebers A, Epstein W. Altendorf K, et al. Ann N Y Acad Sci. 1992 Nov 30;671:228-43. doi: 10.1111/j.1749-6632.1992.tb43799.x. Ann N Y Acad Sci. 1992. PMID: 1288322 Review. No abstract available.
Rapid, high yield purification and characterization of the K(+)-translocating Kdp-ATPase from Escherichia coli.
Siebers A, Kollmann R, Dirkes G, Altendorf K. Siebers A, et al. Among authors: altendorf k. J Biol Chem. 1992 Jun 25;267(18):12717-21. J Biol Chem. 1992. PMID: 1535624 Free article.
The conventional procedure for the purification of the high affinity K+ uptake ATPase (KdpABC) from Escherichia coli involves a tedious three-column protocol (final enzyme purity, approximately 90%; activity yield, 6.5% (Siebers, A., and Altendorf, K. (1988) …
The conventional procedure for the purification of the high affinity K+ uptake ATPase (KdpABC) from Escherichia coli involves a tedio …
187 results