Na+ and K+ Binding by Fulvic Acid
نویسندگان
چکیده
منابع مشابه
Eu(III)-Fulvic Acid Complexation: Evidence of Fulvic Acid Concentration Dependent Interactions by Time-Resolved Luminescence Spectroscopy.
Europium speciation is investigated by time-resolved luminescence spectroscopy (TRLS) in the presence of Suwannee River fulvic acid (SRFA). From complexation isotherms built at different total Eu(III) concentrations, pH values, ionic strength, and SRFA concentrations, it appears that two luminescence behaviors of Eu(III) are occurring. The first part, at the lowest CSRFA values, is showing the ...
متن کاملATP-binding is stabilized by a stacking interaction within the binding site of Na+/K+ -ATPase.
Site-directed mutagenesis was applied to modify phenylalanines (Phe(475)Trp, Phe(548)Tyr, and both) to generate mutants on the basis of molecular modeling of the ATP-binding domain of Na(+)/K(+)-ATPase, in order to characterize the forces that stabilize ATP in its binding pocket. Each of the mutants was examined by Raman difference spectroscopy, i.e., as a difference between the spectrum of the...
متن کاملFound: Na(+) and K(+) binding sites of the sodium pump.
Homology modeling and valence mapping have been used to predict the location and structure of Na(+) and K(+) binding sites in the Na(+)-K(+)-ATPase on the basis of the known atomic resolution structure of SERCA. Additional sites are predicted that may be associated with intracellular access and extracellular egress pathways for Na(+). The model predictions are in excellent agreement with previo...
متن کاملActivation of Na+ and K+ pumping modes of (Na,K)-ATPase by an oscillating electric field.
Serpersu and Tsong (Sepersu, E. H., and Tsong, T. Y. (1983) J. Membr. Biol. 74, 191-201; (1984) J. Biol. Chem. 259, 7155-7162) reported activation of a K+ pumping mode of (Na,K)-ATPase by an oscillating electric field (20 V/cm, 1.0 kHz). Their attempts to activate Na+ pumping at the same frequency were unsuccessful. We report here activation of a Na+ pumping mode with an oscillating electric fi...
متن کاملK+-independent active transport of Na+ by the (Na+ and K+)-stimulated adenosine triphosphatase.
The (Na+ and K+)-stimulated adenosine triphosphatase (Na+,K+)-ATPase) from canine kidney reconstituted into phospholipid vesicles showed an ATP-dependent, ouabain-inhibited uptake of 22Na+ in the absence of added K+. This transport occurred against a Na+ concentration gradient, was not affected by increasing the K+ concentration to 10 microM (four times the endogenous level), and could not be e...
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ژورنال
عنوان ژورنال: Canadian Journal of Chemistry
سال: 1973
ISSN: 0008-4042,1480-3291
DOI: 10.1139/v73-481