Buffers of Low Ionic Strength for Spectrophotometric pK Determinations

1963 ◽  
Vol 16 (4) ◽  
pp. 572 ◽  
Author(s):  
DD Perrin
Keyword(s):  
Ionic Strength ◽  
Constant Ionic Strength ◽  
Ultraviolet Region ◽  
Thermodynamic Quantities ◽  
Small Constant ◽  
Ph Range ◽  
Experimental Values ◽  
Low Ionic Strength

Buffers of low and constant ionic strength (I = 0.01), covering the pH range 2.2 to 11.6 at 20�C, are described. Their near-transparency in the ultraviolet region makes these buffers suitable for spectrophotometric pK determinations, and only small, constant corrections are needed to convert the experimental values to thermodynamic quantities.

scholarly journals A model to explain high values of pH in an alkali sodic soil

2002 ◽  
Vol 59 (4) ◽  
pp. 763-770 ◽  
Author(s):  
José Guerrero-Alves ◽  
Ildefonso Pla-Sentís ◽  
Rafael Camacho
Keyword(s):  
Ionic Strength ◽  
Selectivity Coefficient ◽  
Exchangeable Sodium ◽  
Sodic Soils ◽  
Sodic Soil ◽  
Ion Concentrations ◽  
Hypothetical System ◽  
Predicted Values ◽  
Experimental Values ◽  
Low Ionic Strength

For alkali sodic soils (pH>8.5), the "hydrolysis of exchangeable sodium" has been used as a possible explanation for the alkalinity production and rise in pH of these soils. As an alternative to this hypothesis, a model was developed to simulate and to explain that the alkalinity production and rise in pH is possible in a soil that accumulates alkaline sodium salts and CaCO3. Several simulations were performed by using different combinations of CO2 partial pressures (P), presence or absence of MgCO3, along with experimental values of exchangeable sodium percentage (ESP) and ion concentrations in saturation extracts from an alkali sodic soil (named Pantanal). A hypothetical system with similar conditions to the Pantanal soil but with a Gapon selectivity coefficient (KG) of 0.01475 (mmol L-1)-1/2 was also considered. Good agreement was obtained between experimental and predicted values for pH and ion concentrations in the soil solution when the model (without MgCO3) was applied to the Pantanal soil. However, KG values calculated for the Pantanal soil were generally higher than 0.01475 (mmol L-1)-1/2. Moreover, high pH values and elevated ionic strength were obtained when a KG of 0.01475 (mmol L-1)-1/2 was used at high ESP (similar to those found in the Pantanal soil). KG values obtained for the Pantanal soil and the results obtained in the simulation of the hypothetical system are suggesting that a value higher than 0.01475 (mmol L-1)-1/2 should be used to adequately simulate the behavior of the Pantanal soil at low ionic strength and high ESP values.

scholarly journals The interaction between β-lactoglobulin and sodium N-dodecyl sulphate

1976 ◽  
Vol 153 (3) ◽  
pp. 713-718 ◽  
Author(s):  
M N Jones ◽  
A Wilkinson
Keyword(s):  
Ionic Strength ◽  
Equilibrium Dialysis ◽  
Protein Molecule ◽  
Enthalpies Of Formation ◽  
Enthalpy Of Interaction ◽  
Surfactant Anion ◽  
Ionic Nature ◽  
Ph Range ◽  
Low Ionic Strength ◽  
Β Lactoglobulin

1. The binding of sodium n-dodecyl sulphate to β-lactoglobulin was studied in the pH range 3.5-7.0 by equilibrium dialysis, ultracentrifugation and microcalorimetry. 2. At low binding concentrations (less than 30 bound surfactants anions per protein molecule) the complexes formed aggregates in solution. 3. At higher binding concentrations aggregation does not occur at low ionic strength (0.01 mol/litre), but continues at high ionic strength (0.1 mol/litre). 4. At 25 degrees C the enthalpy of interaction of sodium n-dodecyl sulphate with β-lactoglobulin can be interpreted as the sum of the enthalpies of formation of a complex with 2 bound surfactant anions, with an enthalpy change of -9.5 kJ-mol-1 of bound surfactant, and complexes containing at least 22 bound surfactant anions, with limiting enthalpies per bound surfactant anion of -12.4 kJ-mol-1 at pH 3.5 and -3.25 kJ-mol-1 at pH 5.5. 5. The binding of surfactant and the enthalpy of interaction at pH 3.5 ARE NOT SIGNIFICANTLY AFFECTED BY THE ADDITION Of 8 M-urea. 6. The data indicate that at low binding concentrations the interaction is of an ionic nature, and is accompanied by a conformational change in the protein.

Conformational Transitions in Escherichia coli Ribosomal RNAs as Visualized by Dedicated STEM

1988 ◽  
Vol 46 ◽  
pp. 176-177
Author(s):  
J.S. Wall ◽  
V. Maridiyan ◽  
S. Tumminia ◽  
J. Hairifeld ◽  
M. Boublik
Keyword(s):  
Ionic Strength ◽  
Three Dimensional ◽  
Conformational Transitions ◽  
Dark Field ◽  
Dimensional Structure ◽  
Ribosomal Rnas ◽  
Field Mode ◽  
Freeze Dried ◽  
High Resolution Images ◽  
Low Ionic Strength

The high contrast in the dark-field mode of dedicated STEM, specimen deposition by the wet film technique and low radiation dose (1 e/Å2) at -160°C make it possible to obtain high resolution images of unstained freeze-dried macromolecules with minimal structural distortion. Since the image intensity is directly related to the local projected mass of the specimen it became feasible to determine the molecular mass and mass distribution within individual macromolecules and from these data to calculate the linear density (M/L) and the radii of gyration.2 This parameter (RQ), reflecting the three-dimensional structure of the macromolecular particles in solution, has been applied to monitor the conformational transitions in E. coli 16S and 23S ribosomal RNAs in solutions of various ionic strength.In spite of the differences in mass (550 kD and 1050 kD, respectively), both 16S and 23S RNA appear equally sensitive to changes in buffer conditions. In deionized water or conditions of extremely low ionic strength both appear as filamentous structures (Fig. la and 2a, respectively) possessing a major backbone with protruding branches which are more frequent and more complex in 23S RNA (Fig. 2a).

Adsorption of chlorate and bromate ions on mercury electrodes from constant ionic strength solutions

1988 ◽  
Vol 85 ◽  
pp. 523-527
Author(s):  
M.M. Zuleika ◽  
Palhares SILVA ◽  
Ernesto Rafael GONZALEZ ◽  
Luis Alberto AVACA ◽  
Artur de Jesus MOTHEO
Keyword(s):  
Ionic Strength ◽  
Constant Ionic Strength ◽  
Mercury Electrodes

An Evaluation of a Plasma Fractionation System

1960 ◽  
Vol 4 (01) ◽  
pp. 031-044
Author(s):  
George Y. Shinowara ◽  
E. Mary Ruth
Keyword(s):  
Biological Activity ◽  
Ionic Strength ◽  
Plasma Proteins ◽  
High Concentration ◽  
Significant Evidence ◽  
Native Proteins ◽  
Mobility Data ◽  
Fractionation Procedure ◽  
The Individual ◽  
Low Ionic Strength

SummaryFour primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S20, w and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S20, w classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

Kinetics and Mechanism of Hexachloroiridate(IV) Oxidation of Arsenic(III) in Acidic Perchlorate Solutions

1992 ◽  
Vol 57 (7) ◽  
pp. 1451-1458 ◽  
Author(s):  
Refat M. Hassan
Keyword(s):  
Ionic Strength ◽  
Fractional Order ◽  
Activation Parameters ◽  
Order Reaction ◽  
First Order Reaction ◽  
Intermediate Complex ◽  
Constant Ionic Strength ◽  
Kinetics Of Oxidation ◽  
First Order ◽  
Kinetics Of

The kinetics of oxidation of arsenic(III) by hexachloroiridate(IV) at lower acid concentrations and at constant ionic strength of 1.0 mol dm-3 have been investigated spectrophotometrically. A first-order reaction in [IrCl62-] and fractional order with respect to arsenic(III) have been observed. A kinetic evidence for the formation of an intermediate complex between the hydrolyzed arsenic(III) species and the oxidant was presented. The results showed that decreasing the [H+] is accompanied by an appreciable acceleration of the rate of oxidation. The activation parameters have been evaluated and a mechanism consistent with the kinetic results was suggested.

scholarly journals A novel procedure for the rapid purification of plastocyanin from pea (Pisum sativum) leaves

1981 ◽  
Vol 193 (1) ◽  
pp. 375-378 ◽  
Author(s):  
A R Ashton ◽  
L E Anderson
Keyword(s):  
Ionic Strength ◽  
Pisum Sativum ◽  
Deae Cellulose ◽  
High Concentrations ◽  
Rapid Purification ◽  
Low Ionic Strength

Plastocyanin is soluble at high concentrations (greater than 3 M) of (NH4)2SO4 but under these conditions will adsorb tightly to unsubstituted Sepharose beads. This observation was utilized to purify plastocyanin from pea (Pisum sativum) in two chromatographic steps. Sepharose-bound plastocyanin was eluted with low-ionic-strength buffer and subsequently purified to homogeneity by DEAE-cellulose chromatography.

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