Dissociation constant of acetic acid in N-methylpropionamide from 5 to 55�C and related thermodynamic quantities

1972 ◽  
Vol 1 (6) ◽  
pp. 507-516 ◽  
Author(s):  
Edgar S. Etz ◽  
R. A. Robinson ◽  
Roger G. Bates
Keyword(s):  
Acetic Acid ◽  
Dissociation Constant ◽  
Thermodynamic Quantities

THE DISSOCIATION CONSTANT OF ACETIC ACID FROM 0 TO 35° CENTIGRADE1

1932 ◽  
Vol 54 (4) ◽  
pp. 1350-1357 ◽  
Author(s):  
Herbert S. Harned ◽  
Russell W. Ehlers
Keyword(s):  
Acetic Acid ◽  
Dissociation Constant

Limiting Mobilities of some Monovalent Ions and the Dissociation Constant of Acetic Acid at 25°

Nature ◽  
1933 ◽  
Vol 131 (3297) ◽  
pp. 27-28
Author(s):  
A. I. VOGEL ◽  
G. H. JEFFERY
Keyword(s):  
Acetic Acid ◽  
Dissociation Constant ◽  
Monovalent Ions

THE DISSOCIATION CONSTANT OF ACETIC ACID AND THE ACTIVITY COEFFICIENTS OF THE IONS IN CERTAIN ACETATE SOLUTIONS1

1928 ◽  
Vol 50 (3) ◽  
pp. 696-714 ◽  
Author(s):  
Edwin J. Cohn ◽  
Francis F. Heyroth ◽  
Miriam F. Menkin
Keyword(s):  
Acetic Acid ◽  
Dissociation Constant ◽  
Activity Coefficients

The Dissociation Constant of Acetic Acid in Water-Ethylene Carbonate Mixtures

1990 ◽  
Vol 271 (1) ◽  
Author(s):  
A. A. El-Harakany ◽  
H. Sadek ◽  
A. M. Abdou
Keyword(s):  
Acetic Acid ◽  
Dissociation Constant ◽  
Ethylene Carbonate

scholarly journals A reaction of glucose with peptides

1972 ◽  
Vol 129 (1) ◽  
pp. 203-208 ◽  
Author(s):  
Henry B. F. Dixon
Keyword(s):  
Aqueous Solution ◽  
Acetic Acid ◽  
Blood Glucose ◽  
Dissociation Constant ◽  
Electrophoretic Mobility ◽  
Chemical Properties ◽  
Amino Group ◽  
Half Time ◽  
N Terminus ◽  
And Chemical Properties

Valylhistidine (Val-His) reacts with glucose (Glc) in a mixture of pyridine and acetic acid to form glucosylvalylhistidine (Glc-Val-His). The pK of the α-amino group is thereby lowered to about 5.6 as judged by electrophoretic mobility. The reaction: [Formula: see text] also occurs in an aqueous solution of pyridine and acetic acid of pH6.2 at 50°C, in which it exhibits a half-time of about 30h and a dissociation constant of about 0.3m. Isoleucyltyrosine and glucose react similarly in aqueous solution. The Glc-Val-His has the chromatographic, electrophoretic and chemical properties reported by Holmquist & Schroeder (1966a) for the substance released by proteolysis from the N-terminus of the β-chains of haemoglobin AIc; the value of the dissociation constant means that the concentration of haemoglobin AIc found naturally could be explained by reaction of haemoglobin A with the blood glucose.

scholarly journals Equilibrium and Kinetic Properties of the Interaction between Tetrodotoxin and the Excitable Membrane of the Squid Giant Axon

1970 ◽  
Vol 55 (3) ◽  
pp. 309-335 ◽  
Author(s):  
Leon Andres Cuervo ◽  
William J. Adelman
Keyword(s):  
Dissociation Constant ◽  
Rate Constants ◽  
Sodium Current ◽  
Giant Axon ◽  
Kinetic Properties ◽  
Bathing Solution ◽  
Thermodynamic Quantities ◽  
Partial Recovery ◽  
Reactive Site ◽  
Membrane Complex

Squid giant axons were treated with tetrodotoxin (TTX) in concentrations ranging from 1 nM to 25 nM and the resulting decrease in sodium current was followed in time using the voltage clamp technique. The removal of TTX from the bathing solution produced only partial recovery of the sodium current. This suggests that the over-all interaction is more complex than just a reversible reaction. By correcting for the partial irreversibility of the decrease in sodium current, a dissociation constant of 3.31 x 10-9 M was calculated for the reaction between TTX and the reactive site of the membrane. The data obtained fit a dose-response curve modified to incorporate the correction for partial irreversibility when calculated for a one-to-one stoichiometry. The fit disagreed with that calculated for a reaction between two molecules of TTX with a single membrane-reactive site, but neither supported nor disproved the possibility of a complex formed by two reactive sites with one molecule of TTX. Values of the rate constants for the formation and dissociation of the TTX-membrane complex, k1 and k2, respectively, were obtained from the kinetic data. The values are: k1 = 0.202 x 108 M-1, and k2 = 0.116 min-1. The magnitude of the dissociation constant derived from these values is 5.74 x 10-9 M, which has the same order of magnitude as that obtained from equilibrium measurements. Arrhenius plots of the rate constants gave values for the thermodynamic quantities of activation.

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