Abstract
This article is concerned with two aspects of the structure of Na+/K+-ATPase: the overall quaternary structure of the transport molecule and the function of the N-terminus of the α1-subunit. Selective cleavage of bonds in the α-subunit are important for identifying structure-function relationships of the protein. The N-terminus can be cleaved selectively with trypsin at bond K30-E31 (13,17) and the effects of this truncation on ligand binding, phosphorylation-dephosphorylation, enzymatic (14, 19) and transport reactions (21) have been studied extensively. More recently truncated cDNAs have been expressed in Xenopus oocytes (4,29) for electrophysiological analysis. In this article, this data are evaluated to identify parameters that are relevant for characterization of mutant Na,K-pumps.
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© 1994 Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
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Jørgensen, P.L. (1994). Purified Renal Na+/K+-ATPase; Subunit Structure and Structure-Function Relationships of the N-Terminus of the α1- Subunit. In: Bamberg, E., Schoner, W. (eds) The Sodium Pump. Steinkopff. https://doi.org/10.1007/978-3-642-72511-1_50
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DOI: https://doi.org/10.1007/978-3-642-72511-1_50
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