Pregled bibliografske jedinice broj: 196177
Microenvironment of the high affinity ATP-binding site of Na+/K+-ATPase is slightly acidic
Microenvironment of the high affinity ATP-binding site of Na+/K+-ATPase is slightly acidic // Biochemical and biophysical research communications, 254 (1999), 1; 215-221 (međunarodna recenzija, članak, znanstveni)
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Naslov
Microenvironment of the high affinity ATP-binding site of Na+/K+-ATPase is slightly acidic
Autori
Linnertz, Holger ; Lanz, Edvard ; Gregor, Martin ; Antolović, Roberto ; Krumscheid, Rita ; Obsil, Thomas ; Slavik, Jan ; Kovarik, Željka ; Schoner, Wilhelm ; Amler, Evzen
Izvornik
Biochemical and biophysical research communications (0006-291X) 254
(1999), 1;
215-221
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Na/K-ATPase; FITC; anti-fluorescein; pH; fluorescence dual-excitation
Sažetak
Fluorescein-5'-isothiocyanate (FITC) was used to study the high-affinity ATP-binding site of Na+/K+-ATPase. The molar ratio of specifically bound FITC per alpha-subunit of Na+/K+-ATPase was found to be 0.5 as followed from pretreatment experiments with another specific E1ATP-inhibitor Cr(H2O)4AdoPP[CH2]P. This indicated an existence of one high affinity ATP-binding site (E1ATP-binding site) in the native (alphabeta)2-diprotomer of Na+/K+-ATPase. Fluorescence dual-excitation ratio of specifically bound FITC revealed that at external pH 7.5, the pH value inside the E1ATP-binding site is 6.95 +/- 0.18. In addition, FITC fluorescence quenching by anti-fluorescein and by iodide choline indicated the limited access of water into the small pocket of the E1ATP-binding site. Copyright 1999 Academic Press.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE
