Activity coefficients in (electrolyte + amino acid)(aq) The dependence of the ion-zwitterion interactions on the ionic strength and on the molality of the amino acid analysed in terms of Pitzer's equations

1994 ◽  
Vol 26 (10) ◽  
pp. 1121-1128 ◽  
Author(s):  
R. Rodrı́guez-Raposo ◽  
L. Fernández-Mérida ◽  
M.A. Esteso
1965 ◽  
Vol 20 (6) ◽  
pp. 1332-1336 ◽  
Author(s):  
Edward W. Moore ◽  
James W. Ross

In the investigation of numerous physiological phenomena it is the activity of an ion species which is desired, rather than stoichiometric concentration. The calculation of mean ionic activity from known concentration data requires accurate activity coefficients (ggr). This report concerns the determination of ggrNaCl and ggrCaCl2 in mixed NaCl-CaCl2 solutions by potentiometric measurement with a sodium-selective glass electrode-Ag/AgCl electrode system over the ionic strength range 0.05–0.5 m. Log ggrNaCl varied linearly, at constant total ionic strength, with the ionic strength of CaCl2 in the mixture, in accordance with Harned's rule. From data thus obtained, ggrCaCl2 coefficients in such mixed solutions have been calculated and compared with values calculated from published osmotic data. Resulting activity coefficient curves for ggrCaCl2 are presented over the concentration range encountered in serum and other extracellular fluids. Note: (With the Technical Assistance of Leonard Kaye and Leonard L. Anderson) glass electrodes; ion interaction; electrolyte metabolism; Harned's rule; membrane transport; osmotic coefficients Submitted on March 11, 1965


2004 ◽  
Vol 59 (1) ◽  
pp. 63-72 ◽  
Author(s):  
Mahesha Shetty ◽  
B. Thimme Gowda

Abstract To study the variation of oxidative strengths of N-chloro-arenesulphonamides with substitution in the benzene ring, six mono- and five di-substituted N-chloro-arenesulphonamides are employed as oxidants for studying the kinetics of oxidation of two neutral amino acids, L-leucine and Lisoleucine in aqueous acid medium. The N-chloro-arenesulphonamides studied are of the constitution: ArSO2NaNCl·H2O (where Ar = C6H5, 4-CH3C6H4, 4-C2H5C6H4, 4-FC6H4, 4-ClC6H4, 4-BrC6H4, 2,3-(CH3)2C6H3, 2,4-(CH3)2C6H3, 2-CH3-4-ClC6H3, 2,4-Cl2C6H3, and 3,4-Cl2C6H3). The reactions show second order kinetics in [oxidant], fractional order in [amino acid] and inverse dependence on [H+]. Addition of the reduced product of the oxidants or variation in ionic strength of the medium has no significant effect on the rates of oxidations. A two-pathway mechanism is considered to explain the experimental results. Effective oxidizing species of the oxidants is Cl+ in different forms. Therefore the oxidising strengths of N-chloro-arenesulphonamides depend on the ease with which Cl+ is released from them. The study reveals that the introduction of substituent in the benzene ring of the oxidant affects both the kinetic and thermodynamic data for the oxidations The electron releasing groups such as CH3 generally inhibit the rates, while electron-withdrawing groups such as Cl enhance this ability, as the electron withdrawing groups ease the release of Cl+ from the reagents and hence increase the oxidising strengths. The on Ea and logA and validity of the Hammett and isokinetic relationships for the oxidations are also analysed.


1973 ◽  
Vol 131 (3) ◽  
pp. 541-553 ◽  
Author(s):  
Robert W. Mayes ◽  
Roger M. Mason ◽  
David C. Griffin

1. A proteoglycan fraction (the proteoglycan subunit fraction) was prepared from extracts, with 0.15m-KCl (low-ionic-strength) and 0.5m-LaCl3, 2.0m-CaCl2 and 4.0m-guanidinium chloride (high-ionic-strength), of bovine nasal cartilage by equilibrium-density-gradient centrifugation, essentially as described by Hascall & Sajdera (1969). 2. The use of different centrifugation times showed that near-equilibrium conditions were reached by 48h for the fractions prepared from the high-ionic-strength extracts. The fraction isolated from the low-ionic-strength extract required a longer centrifugation time to reach equilibrium conditions. 3. The composition of the proteoglycan fractions from the various extracts was compared by analyses of their carbohydrate and amino acid contents. Difference indices were calculated from the amino acid analysis to compare the degree of compositional relationship between the protein components of the proteoglycans. 4. Small compositional differences were found between the proteoglycans isolated from the various high-ionic-strength extracts. The protein content of the fractions from the CaCl2 extract and the guanidinium chloride extract showed the greatest difference in this respect, although their amino acid analysis was similar. 5. The proteoglycan fraction isolated from the low-ionic-strength extract shows marked differences in composition from the fractions isolated from the high-ionic-strength extracts. Its protein and glucosamine contents were lower whereas its hexuronic acid and galactosamine contents were higher than those of the latter. It also exhibits major differences in its amino acid composition. The glucosamine:galactosamine ratio of the fraction from the low-ionic-strength extract indicates that it may be an almost exclusively chondroitin sulphate–proteoglycan. Its analysis correlates closely with that of a low-molecular-weight proteoglycan isolated from pig laryngeal cartilage by Tsiganos & Muir (1969). 6. The proteoglycan fractions from both the low- and high-ionic-strength extracts migrate as a single band in zone electrophoresis carried out in a sucrose-density gradient at both pH3.0 and pH7.0, although each showed evidence of band widening during the electrophoresis. All the proteoglycan fractions migrated with the same electrophoretic mobility at pH3.0, irrespective of the differences in composition between them. 7. The differences between the proteoglycans from the low- and high-ionic-strength extracts are discussed and the view is advanced that they may be due to association between predominantly chondroitin sulphate–proteoglycans and a keratan sulphate-enriched proteoglycan species.


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