Lifetimes of oxocarbenium ions in aqueous solution from common ion inhibition of the solvolysis of .alpha.-azido ethers by added azide ion

1989 ◽  
Vol 111 (20) ◽  
pp. 7888-7900 ◽  
Author(s):  
Tina L. Amyes ◽  
William P. Jencks
Keyword(s):  
Aqueous Solution ◽  
Azide Ion ◽  
Oxocarbenium Ions ◽  
Common Ion

ChemInform Abstract: Luminescence Lifetime of Lanthanoid(III) Ions in Aqueous Solution Containing Azide Ion.

ChemInform ◽  
2010 ◽  
Vol 32 (42) ◽  
pp. no-no
Author(s):  
Stefan Lis ◽  
Takaumi Kimura ◽  
Zenko Yoshida
Keyword(s):  
Aqueous Solution ◽  
Luminescence Lifetime ◽  
Azide Ion

Luminescence lifetime of lanthanide(III) ions in aqueous solution containing azide ion

2001 ◽  
Vol 323-324 ◽  
pp. 125-127 ◽  
Author(s):  
Stefan Lis ◽  
Takaumi Kimura ◽  
Zenko Yoshida
Keyword(s):  
Aqueous Solution ◽  
Luminescence Lifetime ◽  
Azide Ion

scholarly journals Photolysis of the azide ion in aqueous solution

1989 ◽  
Vol 17 (1) ◽  
pp. 67
Author(s):  
K. Tennakone ◽  
O. A. Illeperuma ◽  
S. Punchihewa ◽  
A. C. Jayasuriya ◽  
A. H. Jayatissa
Keyword(s):  
Aqueous Solution ◽  
Azide Ion

Efficient Removal of Sulfuric Acid from Sodium Lactate Aqueous Solution Based on the Common-Ion Effect for the Absorption of SO2 of Flue Gas

2019 ◽  
Vol 33 (5) ◽  
pp. 4395-4400 ◽  
Author(s):  
Zhangjin Wu ◽  
Yucui Hou ◽  
Weize Wu ◽  
Shuhang Ren ◽  
Kai Zhang
Keyword(s):  
Aqueous Solution ◽  
Sulfuric Acid ◽  
Flue Gas ◽  
Sodium Lactate ◽  
Efficient Removal ◽  
Common Ion ◽  
The Common ◽  
Common Ion Effect

scholarly journals MEMBRANE POTENTIALS AND CATAPHORETIC POTENTIALS OF PROTEINS

1923 ◽  
Vol 5 (4) ◽  
pp. 505-519 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Aqueous Solution ◽  
Isoelectric Point ◽  
Membrane Potentials ◽  
Double Layers ◽  
Protein Solutions ◽  
Protein Gel ◽  
Low Concentrations ◽  
Alkaline Side ◽  
Common Ion ◽  
Protein Particles

1. It has been shown in preceding publications that the membrane potentials of protein solutions or gels are determined by differences in the concentration of a common ion (e.g. hydrogen ion) inside a protein solution or protein gel and an outside aqueous solution free from protein, and that the membrane potentials can be calculated with a good degree of accuracy from Donnan's equation for membrane equilibria. 2. On the basis of the theory of electrical double layers developed by Helmholtz, we are forced to assume that the cataphoretic potentials of protein particles are determined by a difference in the concentration of the two oppositely charged ions of the same electrolyte in the two strata of an electrical double layer surrounding the protein particle but situated entirely in the aqueous solution. 3. The membrane potentials of proteins agree with the cataphoretic potentials in that the sign of charge of the protein is negative on the alkaline side and positive on the acid side of the isoelectric point of the protein in both membrane potentials and cataphoretic potentials. The two types of potential of proteins disagree, especially in regard to the action of salts with trivalent and tetravalent ions on the sign of charge of the protein. While low concentrations of these salts bring about a reversal of the sign of the cataphoretic potentials of protein particles (at least in the neighborhood of the isoelectric point), the same salts can bring the membrane potentials of proteins only to zero, but call bring about no or practically no reversal of the sign of charge of the protein. Where salts seem to bring about a reversal in the membrane potential of protein solutions, the reversal is probably in reality always due to a change in the pH. 4. We may state, as a result of our experiments, that the cataphoretic migration and the cataphoretic P.D. of protein particles or of suspended particles coated with a protein are the result of two groups of forces; namely, first, forces inherent in the protein particles (these forces being linked with the membrane equilibrium between protein particles and the outside aqueous solution); and second, forces inherent entirely in the aqueous solution surrounding the protein particles. The forces inherent in the protein particles and linked with the membrane equilibrium prevail to such an extent over the forces inherent in the water, that the sense of the cataphoretic migration of protein particles is determined by the forces resulting from the membrane equilibrium.

ChemInform Abstract: Azide Ion Trapping and Lifetime in Aqueous Solution of a Primary Carbenium Ion Stabilized by a 2-Imidazoyl Ring.

ChemInform ◽  
1989 ◽  
Vol 20 (46) ◽  
Author(s):  
J. L. BOLTON ◽  
R. A. MCCLELLAND
Keyword(s):  
Aqueous Solution ◽  
Ion Trapping ◽  
Azide Ion ◽  
Carbenium Ion
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