Dependence Of Kd Research Articles

Cesium Sorption Rate on Non-crushed Rock Measured by a New Apparatus based on a Micro-channel-reactor Concept

AbstractSince nuclide migration through rock mediums is an extremely slow process, experimental effort to evaluate the barrier performance of geologic disposal such as the diffusion coefficient (De) and the distribution coefficient (Kd) requires relatively long testing periods and chemically stable conditions. We have developed a fast method to determine both De and Kd by using a non-crushed rock sample. In this method, a fluoroplastic plate with a micro channel (10-200-μm depth) is placed just beneath a rock-sample plate, and a radionuclide solution is injected into the channel at constant rate. A part of radionuclide diffuses into the rock matrix and/or adsorb on the rock surface. The difference between the inlet and outlet radionuclide flux is simply related to the apparent diffusion coefficient (Da) of the rock sample. In this study, we estimated Kd of Cs for granite by using the equilibrium model, finding that Kd decreased with increasing flow rate. This dependence of Kd on flow rate implies the state of sorption equilibrium. The adsorption and desorption curves of 134Cs were thus measured, and the rate constants for both processes were obtained by adopting a first-order rate law. The rate constants of sorption (k+) and desorption (k-) were obtained as a function of flow velocity; constant values of both were observed. Kd was calculated from k+/ k- and then compared with that determined by conventional batch sorption method using a crushed rock sample. The Kd values determined by the present and conventional methods are in good accordance; however, the testing periods for each method are very different, namely, 1 day and 7 days, respectively.

Metal-Containing Zeolites as Sorbents for Localization of Radioiodine and CsI Aerosols from Vapor-Air and Aqueous Phases

New sorbents for efficient sorption of radioiodine and radiocesium from the vapor-gas phase and aqueous solutions were prepared by treatment of Cu+- and Ag+-substituted NaX and NaA zeolites with acetylene in aqueous solution. The distribution factor Kd of radioiodine and radiocesium between the modified sorbents and aqueous solutions is higher than 103-104 ml g-1. Decontamination factor of the vapor-gas phase with respect to radioiodine and 137CsI aerosols exceeds 102-103 and 103, respectively. The sorption properties of the modified sorbents in both aqueous solutions and the vapor-gas phase are better than those of the initial sorbents. However, localization of radioiodine from the vapor-gas phase with the Cu+-containing sorbents is less efficient than with the Ag+-containing zeolites. At the same time, in aqueous solutions the sorption capacity of the Cu+-containing sorbents for radioiodine is appreciably higher than that of the Ag+-containing sorbents. The sorption properties of the modified sorbents were studied as influenced by various factors. Paracomplexes of univalent copper and silver with C2H2, H2O, and anions present in the solution are probably formed during modification of the metal-containing zeolites. The dependence of Kd of radioiodine on the metal concentration in the sorbent, the free pore volume of the sorbent, and the anion nature was revealed.

Rigorous Formula for the Mean Lifetime of Diffusion-Influenced Second-Order Reactions in Solution: Calculation for Excitation-Transfer Reactions

In second-order reactions in solution where a species of molecules R is subject to reaction with another species S during mutual diffusion, the inverse of the mean lifetime (given by the mean first passage time) of R is linear in the concentration of S when it is sufficiently small. When the concentration of R is also small, the coefficient in the linearity, giving an average rate constant, can rigorously be expressed by 1/(kTST-1 + kD-1) where kTST represents the rate constant expected from the transition-state theory (TST) and is independent of the diffusion constant D, while the D dependence is carried by kD (>0) which decreases as D decreases (Sumi, H. J. Chem. Phys. 1994, 100, 8825). A convenient method for calculating kD has been given for general forms of the mutual-distance (r) dependent interaction potential U(r) and intrinsic reactivity k(r) between R and S. The method was utilized to calculate the D dependence of kD in the entire D region for a long-ranged k(r) ∝ r-6 with U(r) = 0, appropriate ...

The N-terminal B-domain of T4 gene 32 protein modulates the lifetime of cooperatively bound Gp32-ss nucleic acid complexes.

The N-terminal basic or B-domain (residues 1-21) of bacteriophage T4 gene 32 protein (gp32) provides a major determinant for highly cooperative binding by gp32 to single-stranded (ss) nucleic acids at equilibrium. In order to gain mechanistic insight into N-terminal domain function, the kinetics of dissociation of wild-type and previously characterized B-domain substitution mutant gp32s (R4K, R4Q, and K3A) from the model ribohomopolymer, poly(A), have been investigated under solution conditions identical to those used for equilibrium studies [Villemain, J. L., & Giedroc, D. P. (1993) Biochemistry 32, 11235-11246; Villemain, J. L., & Giedroc, D. P. (1996) J. Biol. Chem. 271, 27623-27629]. The dissociation of cooperatively bound gp32-poly(A) complexes was induced by sodium chloride concentration jumps and monitored by an increase in tryptophan fluorescence upon dissociation of the protein from poly(A) using stopped-flow techniques. The apparent dissociation rate constant, kd(app), for all mutant proteins studied was found to depend strongly on the initial fractional saturation of poly(A) just as was found previously for wild-type gp32. This permitted application of Lohman's model for the irreversible dissociation of cooperatively bound gp32-nucleic acid complexes [Lohman, T. M. (1983) Biopolymers 22, 1697-1713] from which the molecular rate constant, ke, the rate of dissociation of a protein monomer from teh end of a gp32-ss nucleic acid complex or protein cluster, could be determined. From the [NaCl]-dependence of kd(app), ke determined at 0.45 M NaCl, pH 8.1, 20 degrees C, was found to be 62 +/- 23, 78 +/- 8, 328 +/- 36, and 384 +/- 34 s-1 for wild-type, R4K, K3A, and R4Q gp32s, respectively. With the exception of R4K gp32, we find a striking correlation between the relative magnitudes of ke and Kapp, suggesting that the molecular defect in the equilibrium binding properties of the N-terminal domain mutants resides in the increased rate at which gp32 monomers dissociate from singly contiguous binding sites at the ends of clusters. The bimolecular association rate constant measured for wild-type gp32 and a weakly binding B-domain mutant, R4T gp32, to poly(dT) was found to be nearly identical, further evidence that the primary defect is in the dissociation reaction. We conclude that the N-terminal domain strongly modulates the lifetime of cooperatively bound gp32-polynucleotide complexes. The mechanistic and functional implications of these findings are discussed.

Kinetic and Thermodynamic Analysis of RNA-Protein Interactions in the RNase P Holoenzyme from Escherichia coli

A gel retardation assay has been used to examine the kinetic and equilibrium properties of the interaction between C5 protein and M1 RNA in the formation of the ribonuclease P holoenzyme from Escherichia coli. The interaction is relatively insensitive to the identity of the monovalent anions present and to pH in the range 7.0-9.0, but it has a more critical requirement for specific monovalent and divalent cations: NH4+, K+, Mg2+, Ca2+, and Mn2+ all promote efficient formation of the complex. A positive delta S (+6.4 cal mol-1 deg-1) and a negative delta H (-11.3 kcal mol-1) combine to give a delta G equal to -13.3 kcal mol-1 at 37 degrees C in 0.42 M salt. The binding reaction is sensitive to the concentration of monovalent and divalent cations, with the affinity increasing with increasing ionic strength (delta log Ka/delta log [NH4+] = +2.7 +/- 0.1). The dependence of Kd on the ionic strength and the positive delta S suggests that hydrophobic and stacking interactions contribute significantly to the formation of the RNase P holoenzyme.

Pressure-induced dissociation of fluorescein from the anti-fluorescein single-chain antibody 4-4-20.

Hydrostatic pressure was used to dissociate fluorescein (Fl) from the high-affinity anti-Fl single-chain antibody 4-4-20 (SCA 4-4-20). Fl dissociation was monitored by measuring (1) the shift in the Fl absorption peak, (2) the recovery in Fl fluorescence intensity, which is quenched upon SCA binding, or (3) the decrease in Fl fluorescence polarization. Pressure effects were studied at two different Fl:SCA 4-4-20 molar ratios: 1:1, at which Fl fluorescence quenching was ca. 35% at atmospheric pressure, and 1:5, at which quenching reached 95-97% under the same conditions. In both cases, pressure-induced dissociation was favored by concomitant dilution of protein and ligand. Dissociation constants (KD) at each pressure were calculated on the basis of measurements of Fl fluorescence polarization under pressure. The dependence of KD, and consequently of delta G of dissociation, on pressure permitted calculation of the magnitude of the standard volume change (delta V) involved in the dissociation process. According to this study, delta V of dissociation for the Fl-SCA complex is -50 mL/mol, which corresponds to a 10-times higher value than that found for dissociation of Fl from the intact IgG mAb 4-4-20 [Herron, J. N., Kranz, D. M., Jameson, D. M., & Voss, E. W., Jr. (1986) Biochemistry 25, 4602-4609]. This difference is explained in terms of a higher overall flexibility of unliganded SCA and of a less stable binding site in SCA relative to mAb.(ABSTRACT TRUNCATED AT 250 WORDS)

X-ray diffraction study of Fe2+-Mg order-disorder in orthopyroxene. Some kinetic results

Kinetic rates of Fe2+-Mg disordering in three orthopyroxenes (mean value of XFe = Fe2+/(Fe2++Mg) = 0.175,0.482,0.770 respectively) have been determined employing heating experiments and single crystal X-ray structural refinements. Disordering rate constants \((\vec K)\) (550800° C) for two pyroxenes are given by: ln \((\vec K)\) = 27.107(±5.177)−32062(±783)T−1(XFe = 0.175) ln \((\vec K)\) = 16.142(±0.057)−18227(±423)T−1(XFe = 0.770) The distribution coefficients KD (representing a steady state of disordering FeM2 + MgM1 ⇋ FeM1 + MgM2) are given by: ln KD = 5.016(±0.223)-7033(±1473) T−1(XFe = 0.175) ln KD = 1.988(±0.122)-3809(±913)T−1(XFe = 0.770) These distribution coefficients provide the constraint of the disordering reaction on the value of the equilibrium constant for Fe2+-Mg order-disorder. Until the low temperature dependence of KD is well constrained, the calculation of cooling rates of pyroxenes and host rocks cannot be done reliably.

Interaction of gelatin with a fluorescein-labeled 42-kDa chymotryptic fragment of fibronectin.

A 42-kDa gelatin binding fragment of human plasma fibronectin was labeled with fluorescein and its fluid-phase interaction with gelatin was investigated. At 25 degrees C in 0.1 M Tris, 0.15 M NaCl, pH 7.3, a dissociation constant, Kd = 0.6 microM, was obtained from the dependence of fluorescence polarization on gelatin concentration. An identical value was obtained for the unlabeled fragment by competition. Binding was unaffected by higher concentrations of NaCl up to 1.0 M, but increased as much as 20-fold at low ionic strength. The dependence of Kd on temperature revealed that dissociation of the complex is accompanied by an increase in entropy. Thus, the interaction is not dominated by either hydrophobic or electrostatic forces; an important role for hydrogen binding is proposed.

Kinetic properties of binding of myosin subfragment-1 with F-actin in the absence of nucleotide.

The rate constant for the binding of myosin subfragment-1 (S-1) with F-actin in the absence of nucleotide, k1, and that for dissociation of the F-actin-myosin subfragment-1 complex (acto-S-1), k-1, were measured independently. The rate of S-1 binding with F-actin was measured from the time course of the change in the light scattering intensity after mixing S-1 with various concentrations of F-actin and k1 was found to be 2.55 X 10(6) M-1 X S-1 at 20 degrees C. The dissociation rate of acto-S-1 was determined using F-actin labeled with pyrenyl iodoacetamide (Pyr-FA). Pyr-FA, with its fluorescence decreased by binding with S-1, was mixed with acto-S-1 complex and the rate of displacement of F-actin by Pyr-FA was measured from the decrease in the Pyr-FA fluorescence intensity. The k-1 value was calculated to be 8.5 X 10(-3) S-1 (or 0.51 min-1). The value of the dissociation constant of S-1 from acto-S-1 complex, Kd, was calculated from Kd = k-1/k1 to be 3.3 X 10(-9) M at 20 degrees C. Kd was also measured at various temperatures (0-30 degrees C), and the thermodynamic parameters, delta G degree, delta H degree, and delta S degree, were estimated from the temperature dependence of Kd to be -11.3 kcal/mol, +2.5 kcal/mol, and +47 cal/deg . mol, respectively. Thus, the binding of the myosin head with F-actin was shown to be endothermic and entropy-driven.

Implications to garnet-clinopyroxene geothermometry of non-ideal solid solution in jadeitic pyroxenes

Garnet-clinopyroxene geothermometry has been applied to numerous rock types from the blueschist and eclogite terrain of the Sesia zone in the Western Alps. Discrepancies in apparent temperatures of up to 600° C have been found suggesting substantial deviation from ideal behaviour of the garnet-clinopyroxene equilibria in certain assemblages. Assemblages containing jadeitic pyroxenes rather than omphacitic or diopsidic pyroxenes yield very low KD (2.0) values and correspondingly high apparent temperatures (> 1,000° C). The garnets coexisting with high-Na pyroxenes have compositions similar to those coexisting with omphacitic pyroxenes. Departure from ideal behaviour of these garnets is likely to be minor and is accomodated in the formulation of the geothermometer. Numerous examples of coexisting garnet-clinopyroxene pairs indicate that there is no obvious relationship of KD with jadeite content in pyroxenes with jadeite content less than ∼70%, but at higher values, KD varies inversely with the jadeite content. The dependence of KD upon the jadeite content in the high-Na pyroxenes is believed to be due to the preference of M2 sites for Fe2+ in the enstatite-jadeite substitution (Fe2+MgNa−1Al−1). This substitution is usually very limited and has no demonstrable effect upon X Fe Cpx when the M1 (Fe2++Mg) content of the pyroxenes is high as in omphacitic and diopsidic pyroxenes. However, when the M1 (Fe2++Mg) content is low, as in jadeitic pyroxenes, the non-ideality of the enstatite type exchange has a marked effect on X Fe Cpx and consequently on garnet-clinopyroxene calculations.

Kinetic of potash alum crystallisation

AbstractMetastable zone width of potash alum in aqueous solutions has been measured as function of the cooling rate in absence as well as in presence of seed crystals. From these data, the effective nucleation rate was calculated. Growth rate of potash alum crystals has been measured in a fluidized bed. Overall growth rate coefficient, kG, was then used for determination of the mass transfer coefficient, kD, and the rate constant of the intergration step kr. The dependence of kD on hydrodynamic conditions is discussed.