Electrophoretic mobility and computations of solid-aqueous solution equilibria for the bastnaesite-H2O system

2013 ◽  
Vol 30 (1) ◽  
pp. 18-23 ◽  
Author(s):  
R. Herrera-Urbina ◽  
Pradip ◽  
D. W. Fuerstenau
Keyword(s):  
Aqueous Solution ◽  
Electrophoretic Mobility ◽  
Solution Equilibria

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 Carboxylate Complexing of Iron(III). I. The Formation of Monoacetatoiron(III) in Aqueous Solution: Equilibria and Kinetics

1972 ◽  
Vol 50 (2) ◽  
pp. 194-200 ◽  
Author(s):  
R. N. Pandey ◽  
W. MacF. Smith
Keyword(s):  
Aqueous Solution ◽  
Ionic Strength ◽  
Kinetic Studies ◽  
Solution Equilibria ◽  
Independent Reaction

The kinetics and equilibria involved in the formation of monoacetatoiron(III) from iron(III) in aqueous solution has been investigated at ionic strength 0.50 M and temperatures ranging from 5.2 to 25 °C for kinetic studies and 5.2 to 41 °C for equilibria. The results support the view that the mechanism of the acid independent reaction involves the reactants FeOH2+ and CH3COOH in an interchange dissociative (Id) mechanism with ΔH≠ = 11.1 ± 2.2 kcal mol−1. The nature of the acid dependent reactions remains unresolved.

scholarly journals Effect of pH on the Electrophoretic Mobility of Spores of Bacillus anthracis and Its Surrogates in Aqueous Solutions

2012 ◽  
Vol 78 (23) ◽  
pp. 8470-8473 ◽  
Author(s):  
Colin P. White ◽  
Jonathan Popovici ◽  
Darren A. Lytle ◽  
Noreen J. Adcock ◽  
Eugene W. Rice
Keyword(s):  
Aqueous Solution ◽  
Bacillus Anthracis ◽  
Electrophoretic Mobility ◽  
Rrna Gene ◽  
Phylogenetic Clustering ◽  
Content Type ◽  
Transport Studies ◽  
Surrogate Selection ◽  
Ph Range ◽  
The 16S Rrna Gene

ABSTRACTThe electrophoretic mobility (EPM) of endospores ofBacillus anthracisand surrogates was measured in aqueous solution across a broad pH range and several ionic strengths. EPM values trended around phylogenetic clustering based on the 16S rRNA gene. Measurements reported here provide new insight forBacillus anthracissurrogate selection and for attachment/detachment and transport studies.

The Interaction of Cigarette Smoke Solution with α1-Antitrypsin: Effect on Inhibitory Capacity, Electrophoretic Mobility and Immunological Measurement

1983 ◽  
Vol 64 (2) ◽  
pp. 223-230 ◽  
Author(s):  
Robert A. Stockley ◽  
Simon C. Afford
Keyword(s):  
Aqueous Solution ◽  
Oxidative Damage ◽  
Electrophoretic Mobility ◽  
Cigarette Smoke ◽  
Protein Concentration ◽  
Inhibitory Capacity ◽  
Pure Protein

1. The effects of an aqueous solution of cigarette smoke upon the functional, immunological and electrophoretic assessment of α1-antitrypsin have been studied. 2. The addition of cigarette smoke reduced the inhibitory capacity of the α1-antitrypsin and this was associated with at least a 22% underestimation of the protein concentration by immunological measurement. 3. Furthermore the cigarette-smoke-damaged α1-antitrypsin had an increased electrophoretic mobility in plain agarose compared with the pure protein and was more susceptible to proteolytic damage by elastase. 4. Comparison with results obtained in vivo suggests that oxidative damage to α1-antitrypsin is not the only mechanism involved in the reduction of its inhibitory capacity in secretions, even in non-smokers.

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