FEBS Letters | |
Functional expression of N‐terminal truncated α‐subunits of Na,K‐ATPase in Xenopus laevis oocytes | |
Geering, Käthi1  Burgener-Kairuz, Pauline1  Rossier, Bernard C.1  Horisberger, Jean-Daniel1  | |
[1] Institut de Pharmacologie et de Toxicologie, Université de Lausanne, Bugnon 27, CH-1005 Lausanne, Switzerland | |
关键词: Na; K-pump; Ouabain binding; Potassium activation; α1 Isoform; β3 Isoform; | |
DOI : 10.1016/0014-5793(91)81231-V | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
N-terminal deletion mutants of Na,K-ATPase α1 isoforms initiating translation at Met34 (α1T1) or at Met43 (α1T2) were expressed in X. laevis oocytes. Compared to β3 cRNA injected controls, the co-expression of α1wt, α1T1, α1T2 with β3 subunits results in a 2- to 3-fold increase of ouabain binding sites, parallelled by a concomitant increase in Na,K-pump current. The apparent K½ for potassium activation of the α1T2/β3 Na,K-pumps is significantly higher than that of the α1wt/β3 or α1T1/β3 Na,K-pumps expressed at the cell surface. Total deletion of the lysine-rich N-terminal domain thus allows the expression of active Na,K-pump but with distinct cation transport properties.
【 授权许可】
Unknown
【 预 览 】
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RO201912020295357ZK.pdf | 655KB | download |