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And ionic strength

Most of the Langmuir films we have discussed are made up of charged amphiphiles such as the fatty acids in Chapter IV and the lipids in Sections XV-4 and 5. Depending on the pH and ionic strength of the subphase, electrostatic effects can become quite important. Here we develop the theoretical foundation for charged films with the Donnan relationship. Then we mention the influence of subphase pH on film behavior. [Pg.553]

One potentially powerfiil approach to chemical imaging of oxides is to capitalize on the tip-surface interactions caused by the surface charge induced under electrolyte solutions [189]. The sign and the amount of the charge induced on, for example, an oxide surface under an aqueous solution is detenuined by the pH and ionic strength of the solution, as well as by the isoelectric point (lEP) of the sample. At pH values above the lEP, the charge is negative below this value. [Pg.1714]

A cubic lattice is superimposed onto the solute(s) and the surrounding solvent. Values of the electrostatic potential, charge density, dielectric constant and ionic strength are assigned to each grid point. The atomic charges do not usually coincide with a grid point and so the... [Pg.620]

Eactors that could potentiaHy affect microbial retention include filter type, eg, stmcture, base polymer, surface modification chemistry, pore size distribution, and thickness fluid components, eg, formulation, surfactants, and additives sterilization conditions, eg, temperature, pressure, and time fluid properties, eg, pH, viscosity, osmolarity, and ionic strength and process conditions, eg, temperature, pressure differential, flow rate, and time. [Pg.140]

Hydrolysis constants for Pu(IV) have been determined in aqueous solutions at many pH values and ionic strengths. In 1 Af NaClO solution the first three Pu(IV) — OH complexes and overall stabiUty constants are (105) as follows ... [Pg.199]

Retention and stereoselectivity on the BSA columns can be changed by the use of additives to the aqueous mobile phase (30). Hydrophobic compounds generally are highly retained on the BSA, and a mobile-phase modifier such as 1-propanol can be added to obtain reasonable retention times. The retention and optical resolution of charged solutes such as carboxyUc acids or amines can be controlled by pH and ionic strength of the mobile phase. [Pg.100]

Protease performance is strongly influenced by detergent pH and ionic strength. Surfactants influence both protease performance and stabiUty in the wash solution. In general, anionic surfactants are more aggressive than amphoteric surfactants, which again are more aggressive than nonionic surfactants. [Pg.294]

Kinetic mles of oxidation of MDASA and TPASA by periodate ions in the weak-acidic medium at the presence of mthenium (VI), iridium (IV), rhodium (III) and their mixtures are investigated by spectrophotometric method. The influence of high temperature treatment with mineral acids of catalysts, concentration of reactants, interfering ions, temperature and ionic strength of solutions on the rate of reactions was investigated. Optimal conditions of indicator reactions, rate constants and energy of activation for arylamine oxidation reactions at the presence of individual catalysts are determined. [Pg.37]

The protonation equilibria for nine hydroxamic acids in solutions have been studied pH-potentiometrically via a modified Irving and Rossotti technique. The dissociation constants (p/fa values) of hydroxamic acids and the thermodynamic functions (AG°, AH°, AS°, and 5) for the successive and overall protonation processes of hydroxamic acids have been derived at different temperatures in water and in three different mixtures of water and dioxane (the mole fractions of dioxane were 0.083, 0.174, and 0.33). Titrations were also carried out in water ionic strengths of (0.15, 0.20, and 0.25) mol dm NaNOg, and the resulting dissociation constants are reported. A detailed thermodynamic analysis of the effects of organic solvent (dioxane), temperature, and ionic strength on the protonation processes of hydroxamic acids is presented and discussed to determine the factors which control these processes. [Pg.40]

Fig. 8.P28. pH-Ratio profiles for the hydrolysis of alkyl-A/-methylmaleamic acids at 39°C and ionic strength 1.0. In increasing order of reactivity, R = H, Me, Et, i-Pr, t-Bu. Reproduced from problem reference 28 by permission of the Royal Chemical Society. Fig. 8.P28. pH-Ratio profiles for the hydrolysis of alkyl-A/-methylmaleamic acids at 39°C and ionic strength 1.0. In increasing order of reactivity, R = H, Me, Et, i-Pr, t-Bu. Reproduced from problem reference 28 by permission of the Royal Chemical Society.
Fig. 8.P3I. Plot of the pseudo-first-order rate constants for hydrolysis of thioesters A (O), B ( ), C (A), D (A) as a fiinction of pH at 50°C and ionic strength 0.1 (KCI). Lines are from fits of the data to = kon(K /H+)) + (k KJK + [//+])) where koH is the hydroxide term and is the intramolecular assistance term for B and C and from linear regression for A and D. Reproduced from problem reference 31 by permission of the American Chemical Society. Fig. 8.P3I. Plot of the pseudo-first-order rate constants for hydrolysis of thioesters A (O), B ( ), C (A), D (A) as a fiinction of pH at 50°C and ionic strength 0.1 (KCI). Lines are from fits of the data to = kon(K /H+)) + (k KJK + [//+])) where koH is the hydroxide term and is the intramolecular assistance term for B and C and from linear regression for A and D. Reproduced from problem reference 31 by permission of the American Chemical Society.
Tailing peaks or longer than expected elution volumes are sometimes caused by low solubility of the protein in the mobile phase. Using a trial-and-error process, select the proper pFf and ionic strength to address this problem. Detergents such as sodium dodecyl sulfate (SDS) are sometimes helpful but, because they change the conformation of many proteins and are difficult to remove from the column should be used only if other methods fail. [Pg.90]

In the development of a SE-HPLC method the variables that may be manipulated and optimized are the column (matrix type, particle and pore size, and physical dimension), buffer system (type and ionic strength), pH, and solubility additives (e.g., organic solvents, detergents). Once a column and mobile phase system have been selected the system parameters of protein load (amount of material and volume) and flow rate should also be optimized. A beneficial approach to the development of a SE-HPLC method is to optimize the multiple variables by the use of statistical experimental design. Also, information about the physical and chemical properties such as pH or ionic strength, solubility, and especially conditions that promote aggregation can be applied to the development of a SE-HPLC assay. Typical problems encountered during the development of a SE-HPLC assay are protein insolubility and column stationary phase... [Pg.534]

An effective experimental design is to measure the pseudo-first-order rate constant k at constant pH and ionic strength as a function of total buffer concentration 6,. Very often the buffer substance is the catalyst. Let B represent the conjugate base form of the buffer. Because pH is constant, the ratio (B]/[BH ] is constant, and the concentrations of both species increase directly with 6 where B, = [B] -t-[BH"]. [Pg.268]

Figure 6-4. Plol of Eq. (6-46) for the hydrolysis of cinnamic anhydride at 25°C and ionic strength 0.1 M in carbonate buffers. fi, represents the total buffer concentration. From top to bottom, pH = 10.06, 9.76, and 9.14. Figure 6-4. Plol of Eq. (6-46) for the hydrolysis of cinnamic anhydride at 25°C and ionic strength 0.1 M in carbonate buffers. fi, represents the total buffer concentration. From top to bottom, pH = 10.06, 9.76, and 9.14.
Under the conditions of temperature and ionic strength prevailing in mammalian body fluids, the equilibrium for this reaction lies far to the left, such that about 500 CO2 molecules are present in solution for every molecule of H2CO3. Because dissolved CO2 and H2CO3 are in equilibrium, the proper expression for H2CO3 availability is [C02(d)] + [H2CO3], the so-called total carbonic acid pool, consisting primarily of C02(d). The overall equilibrium for the bicarbonate buffer system then is... [Pg.53]

FIGURE 5.16 The solubility of most globular proteins is markedly influenced by pH and ionic strength. This figure shows the solubility of a typical protein as a function of pH and various salt concentrations. [Pg.129]

In many situations, the actual molar amount of the enzyme is not known. However, its amount can be expressed in terms of the activity observed. The International Commission on Enzymes defines One International Unit of enzyme as the amount that catalyzes the formation of one micromole of product in one minute. (Because enzymes are very sensitive to factors such as pH, temperature, and ionic strength, the conditions of assay must be specified.) Another definition for units of enzyme activity is the katal. One katal is that amount of enzyme catalyzing the conversion of one mole of substrate to product in one second. Thus, one katal equals 6X10 international units. [Pg.438]

This simple formula does not apply to pH values over 9 0, and high salinities affect its accuracy. The term (pKj - pKJ is a function of temperature and ionic strength (dissolved solids). In an analysis of a given water at a constant temperature much useful information can be obtained from the equation. [Pg.351]

That the reaction was not catalysed by the buffer anion is shown by the data in Table 197, which gives the rate coefficients observed klob, and the rate coefficients ky corr corrected for difference in pH and ionic strength to values of 6.70 and 0.14 respectively. The existence of the general acid-catalysed mechanism for the reaction was demonstrated by the data in Table 198, which gives the rate coeffi-... [Pg.294]

The kinetics of decarboxylation of 4-aminosalicylic acid in some buffer solutions at 50 °C were studied. The first-order rate coefficients increased with increasing buffer concentration, though the pH and ionic strength were held constant (Table 217). This was not a salt effect since the rate change produced by substituting potassium chloride for the buffer salt was shown to be much smaller. It follows from the change in the first-order rate coefficients (kx) with... [Pg.313]

The reaction follows a mixed second-order rate law. The progress was monitored spec-trophotometrically at 723 nm, where Np4+ has a maximum absorption. The following data refer to an experiment with [Np3+]o = 1.53 x 10-4 M, [Fe3+]o = 2.24 x 10-4 M (taken at 298.0 K, [H+] = 0.400 M, and ionic strength = 2.00 M). Calculate the rate constant either taking the end point value as 0.351 or, if a suitable program is available, allowing it to be found in the calculation. [Pg.41]

Stability constants as a function of temperature and the calculated complexation enthalpies and entropies of the associated reactions are given in Table II. The results of duplicate experiments at 2.0 M acidity and ionic strength are shown as the last entry in the table. Comparison of the results at 25°C, and 1.0 and 2.0 M acidity indicate an approximate inverse first order stoichiometry in [IT "] for the Kj and acid independence for K2. [Pg.256]


See other pages where And ionic strength is mentioned: [Pg.10]    [Pg.915]    [Pg.720]    [Pg.158]    [Pg.528]    [Pg.529]    [Pg.27]    [Pg.32]    [Pg.490]    [Pg.500]    [Pg.403]    [Pg.13]    [Pg.106]    [Pg.442]    [Pg.2057]    [Pg.2059]    [Pg.10]    [Pg.61]    [Pg.279]    [Pg.219]    [Pg.353]    [Pg.410]    [Pg.372]    [Pg.314]    [Pg.27]    [Pg.42]    [Pg.79]   
See also in sourсe #XX -- [ Pg.67 ]




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Effects of Ionic Strength and pH on the Polyelectrolyte Star Conformation

Effects of ionic strength and

Ionic Strength and Debye-Hiickel Theory

Ionic strength

Ionic strength, and dielectric constant

PH and ionic strength, effect

PLIMSTEX in Biologically Relevant Media and High Ionic Strength

Polarity and Ionic Strength

Solution pH and ionic strength

Stoichiometric and Effective Ionic Strength

Temperature and Ionic Strength , Effects on Equilibria Using pC-pH Diagrams

The Carrier Ampholytes, Ionic Strength and Influence on Solubility of Proteins

The ionic strength and non-ideality

Use of cells to determine mean activity coefficients and their dependence on ionic strength

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