Potassium binding to the (Na+ + K+)-ATPase

Autor: J.C. Skou, D. Hastings

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 601:380-385

The number of K+ bound to the ( Na + + K + )- ATPase has been measured under equilibrium conditions by a differential-titration technique (Hastings, D.F. (1977) Anal. Biochem. 83, 416–432). 5.1 K+ were bound per 32P-labelling site. The K′ D for K

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bea68242294564ce0304468de62d1a7b
https://doi.org/10.1016/0005-2736(80)90542-8

Enzymatic aspects of active linked transport of Na+ and K+ through the cell membrane

Autor: J.C. Skou

Publikováno v: Progress in Biophysics and Molecular Biology. 14:131-166

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f97fa18a018770ac9f018cc821545466
https://doi.org/10.1016/s0079-6107(64)80005-5

Effects of ATP and protons on the Na : K selectivity of the (Na+ + K+)-ATPase studied by ligand effects on intrinsic and extrinsic fluorescence

Autor: M. Esmann, J.C. Skou

Publikováno v: Skou, J C & Esmann, M 1980, ' Effects of ATP and protons on the Na : K selectivity of the (Na+ + K+)-ATPase studied by ligand effects on intrinsic and extrinsic fluorescence ', BBA General Subjects, vol. 601, no. 2, pp. 386-402 .

The effect of pH and of ATP on the Na : K selectivity of the ( Na + + K + )- ATPase has been tested under equilibrium conditions. The Na+ : K+-induced change in intrinsic tryptophan fluorescence and in fluorescence of eosin maleimide bound to the sys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6dcf23eab1e861ce18685088f0ebce5
https://pubmed.ncbi.nlm.nih.gov/6157415

Effect on the equilibrium between the Na+-form and the K+-form of the (Na+ + K+)-ATPase of modification of the enzyme with pyridoxal 5-phosphate

Autor: J.C. Skou

Publikováno v: Biochimica et biophysica acta. 789(1)

(1) An increase in pH shifts the equilibrium between the K+-form and the Na+-form of the Na+ + K+-ATPase towards the Na+-form. pK for the proton effect on the equilibrium is decreased by modification of the enzyme with pyridoxal 5-phosphate. (2) The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e282118be0159b6a3f5999942984cfd3
https://pubmed.ncbi.nlm.nih.gov/6087913

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