Quaternary benzyltriethylammonium ion binding to the Na,K-ATPase: A tool to investigate extracellular K+ binding reactions

This study examined how the quaternary organic ammonium ion, benzyltriethylamine (BTEA), binds to the Na,K-ATPase to produce membrane potential (VM)-dependent inhibition and tested the prediction that such a VM-dependent inhibitor would display electrogenic binding kinetics. BTEA competitively inhib...

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Detalles Bibliográficos
Autores principales: Peluffo, R.D., González-Lebrero, R.M., Kaufman, S.B., Kortagere, S., Orban, B., Rossi, R.C., Berlin, J.R.
Formato: JOUR
Materias:
Ammonium ions
ATP-ase activity
Binding kinetics
Binding reactions
Extracellular
Homology models
Initial rate
Ion binding
Ion transports
Membrane potentials
Minimum value
Pump current
Quaternary amines
Similar degree
Step changes
Structural analogue
Transient current
Transmembrane helices
Amines
Ammonium compounds
Binding energy
Binding sites
Electric fault currents
Enzymes
Ions
Optical devices
Rate constants
Ion exchange
adenosine triphosphatase (potassium sodium)
benzyltriethylamine
potassium ion
quaternary ammonium derivative
rubidium ion
unclassified drug
amino acid sequence
animal cell
article
binding competition
controlled study
enzyme activation
enzyme binding
heart muscle fiber membrane
nonhuman
patch clamp
potassium transport
priority journal
rat
transport kinetics
Animals
Binding Sites
Dogs
Electric Conductivity
Enzyme Inhibitors
Extracellular Space
Membrane Potentials
Models, Biological
Models, Molecular
Nitro Compounds
Potassium
Protein Binding
Protein Conformation
Quaternary Ammonium Compounds
Rabbits
Rats
Rubidium
Sodium-Potassium-Exchanging ATPase
Time Factors
Strophanthus gratus
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v48_n34_p8105_Peluffo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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