EPR and water proton relaxation rate ( ] / T i ) studies of partially (40%) and "fully" (90%) purified preparations of membrane-bound (Na' + K+) activated ATPase from sheep kidney indicate one tight binding site for Mn" per enzyme dimer, with a dissociation constant (K,, = 0.88 pM) in agreement with
Studies on the role of sodium- and potassium-activated adenosine triphosphatase inhibition in the pathogenesis of human hypertension
✍ Scribed by Kramer, H. J. ;Gl�nzer, K. ;Freitag, T. ;Sch�nfeld, J. ;Sorger, M. ;Schlebusch, H. ;D�sing, R. ;Kr�ck, F.
- Publisher
- Springer-Verlag
- Year
- 1985
- Tongue
- English
- Weight
- 484 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1432-1440
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The catalytic activity of adenosine-5'-triphosphatase (5'-ATPase), activated by Na+ and K+ ions in the presence of Mg2+ ions, was determined by a direct method using batch microcalorimetry. The enzymatic hydrolysis of S'-ATP in Tris-HCI buffer was used without any auxiliary reaction. The rate of hea
## Abstract Mg^2+^ATPase and (Na^+^K^+^)ATPase activities were measured in clonal line NN hamster astroblasts and in clonal lines M~1~ and N~1E‐115~ mouse neuroblastoma cells after the cells had been subjected to the acute and chronic actions of 100 mM ethanol. Exposure of the astroblasts to ethano