Výsledky vyhledávání

Stimulation by Phorbol 12-Myristate 13-Acetate (PMA) of Na,K-Pump Mediated 86Rb+-Influx Into Human Lymphocytes

Autor: J. G. Nørby, N. Obel

Publikováno v: The Sodium Pump ISBN: 9783642725135

The Na,K-pump in cells is a target for both long-term (latency of 1–24 hours) and acute (seconds-minutes) regulation (5,6). In both cases stimulation or decrease in pumping activity is observed. The subject of this paper is the acute up-regulation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a1236f2318ca6144f26d4cab964feb31
https://doi.org/10.1007/978-3-642-72511-1_123

Zobrazit plný text záznamu

Kinetics of K(+)-stimulated dephosphorylation and simultaneous K+ occlusion by Na,K-ATPase, studied with the K+ congener Tl+. The possibility of differences between the first turnover and steady state

Autor: R C, Rossi, J G, Nørby

Publikováno v: The Journal of biological chemistry. 268(17)

Using the K+ congener Tl+ and rapid mixing combined with special quench techniques, we have investigated (at 20 degrees C) what is usually assumed to be the enzymatic correlate of active transport of K+ by Na,K-ATPase: the Tl(+)-catalyzed dephosphory

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a0a291bba02803700e65ff01138e30bb
https://pubmed.ncbi.nlm.nih.gov/8389760

Zobrazit plný text záznamu

Functional significance of the oligomeric structure of the Na,K-pump from radiation inactivation and ligand binding

Autor: J G, Nørby, J, Jensen

Publikováno v: Society of General Physiologists series. 46

The present article is concerned with the oligomeric structure and function of the Na,K-pump (Na,K-ATPase). The questions we have addressed, using radiation inactivation and target size analysis as well as ligand binding, are whether the minimal stru

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::74ebbc63452816c88bb4fd9b980b647b
https://pubmed.ncbi.nlm.nih.gov/1653978

Zobrazit plný text záznamu

A model for the stepwise radiation inactivation of the alpha 2-dimer of Na,K-ATPase

Autor: J G, Nørby, J, Jensen

Publikováno v: The Journal of biological chemistry. 264(33)

This study is a direct continuation of Jensen, J., and Nørby, J. G., (1988) J. Biol. Chem. 263, 18063-18070. A new model in which we propose that the in situ organization of the Na,K-ATPase alpha-subunit is an alpha 2-dimer and which describes the s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2bab9c0202cbc2953b72bd98b50cbc19
https://pubmed.ncbi.nlm.nih.gov/2555324

Zobrazit plný text záznamu

Membrane-bound Na,K-ATPase: target size and radiation inactivation size of some of its enzymatic reactions

Autor: J, Jensen, J G, Nørby

Publikováno v: The Journal of biological chemistry. 263(34)

Frozen samples of membrane-bound pig kidney Na,K-ATPase were subjected to target size analysis by radiation inactivation with 10-MeV electrons at -15 degrees C. The various properties investigated decreased monoexponentially with radiation dose, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b61562c1db22464ff67271a6b72f4ed0
https://pubmed.ncbi.nlm.nih.gov/2848022

Zobrazit plný text záznamu

Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour

Autor: P Ottolenghi, J Jensen, J G Nørby

Publikováno v: The Journal of physiology. 346

Using a rate-dialysis technique at 0-2 degrees C, the affinities of Na+ and K+ for the sodium pump of pig kidney outer medulla were determined from their effects on the binding of ADP to the enzyme. Since all experiments were carried out in the prese

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d851b04cb1fe8ea55df4c3c111a95413
https://pubmed.ncbi.nlm.nih.gov/6321716

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání