Potential-pH diagrams for the systems Ir-H2O-Cl-, Pt-H2O-Cl-, and Pd-H2O-Cl- at 25 °C

1990 ◽  
Vol 55 (4) ◽  
pp. 987-993
Author(s):  
Tomáš Loučka ◽  
Zdenko Ternbach

On the basis of available thermodynamic data, potential-pH diagrams have been calculated for the systems Ir-H2O-Cl-, Pt-H2O-Cl-, and Pd-H2O-Cl- in a 264 g/l NaCl aqueous solution at 25 °C.

2010 ◽  
Vol 982 (1-3) ◽  
pp. 62-65 ◽  
Author(s):  
Andreia Neves Fernandes ◽  
Carlos Alberto Policiano Almeida ◽  
Nito Angelo Debacher ◽  
Maria Marta de Souza Sierra

1962 ◽  
Vol 40 (3) ◽  
pp. 363-372 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook

The effect of pH, temperature, ionic strength, and lipoprotein concentration on the reversible dissociation of α- and β-lipovitellin in aqueous solutions above pH 6 has been examined by ultracentrifugal measurements. Under otherwise similar conditions α- and β-lipovitellin are 50% dissociated at pH 10.5 and 7.8, respectively. Both lipovitellins undergo an irreversible aggregation above about pH 11; β-lipovitellin is sometimes converted to a non-dissociable form upon aging. Dissociation of both lipovitellins decreases with increasing ionic strength and increasing temperature. Although the ultracentrifugal method has limitations, provisional equilibrium constants and thermodynamic data were obtained from it that are comparable with those obtained for certain protein systems.


2014 ◽  
Vol 60 (1) ◽  
pp. 192-201 ◽  
Author(s):  
Rosalia Maria Cigala ◽  
Concetta De Stefano ◽  
Anna Irto ◽  
Demetrio Milea ◽  
Silvio Sammartano

1962 ◽  
Vol 40 (1) ◽  
pp. 363-372 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook

The effect of pH, temperature, ionic strength, and lipoprotein concentration on the reversible dissociation of α- and β-lipovitellin in aqueous solutions above pH 6 has been examined by ultracentrifugal measurements. Under otherwise similar conditions α- and β-lipovitellin are 50% dissociated at pH 10.5 and 7.8, respectively. Both lipovitellins undergo an irreversible aggregation above about pH 11; β-lipovitellin is sometimes converted to a non-dissociable form upon aging. Dissociation of both lipovitellins decreases with increasing ionic strength and increasing temperature. Although the ultracentrifugal method has limitations, provisional equilibrium constants and thermodynamic data were obtained from it that are comparable with those obtained for certain protein systems.


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