Zobrazeno 1 - 10
of 165
pro vyhledávání: '"H. -J. Apell"'
Publikováno v:
Journal of Membrane Biology. 156:63-71
The function of the Na,K-ATPase is known to be considerably impaired in the presence of free radicals such as OH.. While previous experiments were largely based on the loss of enzymatic activity of the protein, this is the first communication dealing
The changes in capacitance and conductance of lipid bilayer membranes have been studied with adsorbed membrane fragments containing Na+,K+-ATPase. These changes have been initiated by fast release of protons from a bound form (“caged H+”) induced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::339cc0d7d64042abe5f6217121da6048
Publikováno v:
Biophysical Journal. 61(1):83-95
In this paper the electrostatic interactions between membrane-embedded ion-pumps and their consequences for the kinetics of pump-mediated transport processes have been examined. We show that the time course of an intrinsically monomolecular transport
Autor:
H.-J. Apell, Michael Habeck
Publikováno v:
Biophysical Journal. 96(3)
Electrochromic styryl dyes are in use now for almost two decades to detect ion movements in various P-type ATPases. The extremely hydrophobic dye molecules have a high partition coefficient in favor of the hydrophobic core of lipid phase of membrane
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1023:81-90
Na,K-ATPase from rabbit kidney outer medulla was reconstituted in large unilamellar lipid vesicles by detergent dialysis. Vesicles prepared in the presence or absence of potassium allowed to study two different transport modes: the (physiological) Na
Autor:
H-J, Apell
Publikováno v:
Reviews of physiology, biochemistry and pharmacology. 150
P-type ATPases are a large family of membrane proteins that perform active ion transport across biological membranes. In these proteins the energy-providing ATP hydrolysis is coupled to ion-transport that builds up or maintains the electrochemical po
Publikováno v:
The Journal of biological chemistry. 275(3)
Based on the following observations we propose that the cytoplasmic loop between trans-membrane segments M6 and M7 (L6/7) of the alpha subunit of Na(+),K(+)-ATPase acts as an entrance port for Na(+) and K(+) ions. 1) In defined conditions chymotrypsi
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 643
The complex functions of the Na,K-ATPase can be described by reaction cycles based on the generally accepted "Post-Albers cycle". By appropriate experimental conditions various, partly overlapping partial reactions may be isolated which allow the inv
Publikováno v:
Biophysical chemistry. 72(3)
The intrinsic fluorescence emission kinetics of Na,K-ATPase, a large membrane protein containing 16 tryptophan residues, was studied by time-resolved techniques. The lifetime distributions recovered by the Maximum Entropy Method exhibit a strong depe
Publikováno v:
Membranecell biology. 11(5)
The goal of work was to investigate the electrogenic transport of Na ions by Na+,K(+)-ATPase in membrane fragments absorbed on a planar bilayer lipid membrane. The photorelease of ATP from an inactive precursor, caged ATP, induced a transient current