SEARCH · PubMed Health

Results for “Kinetics”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources

PubMed1994

Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect.

CheY, the 129 amino acid chemotactic protein from Escherichia coli, is a good model for studying the folding process of the parallel alpha/beta family of proteins. A study of the folding kinetics of CheY using fluorescence and far-UV circular dichroism (CD) stopped-flow measurements is reported. CheY has three prolines, two of them in the trans conformation and one, Pro110, with a cis Lys-Pro peptide bond. This protein presents a unimolecular, but complex, kinetic mechanism that is dominated by a slow phase compatible with a trans-cis isomerization. Mutation of Pro110 to Gly results in the disappearance of this slow phase, indicating that this cis prolyl bond is responsible for it. The slow phase is catalyzed in a very inefficient way by prolyl isomerase, indicating that the cis bond is poorly accessible to the enzyme during refolding. In agreement with this is the fact that the isomerization of the Lys109-Pro110 bond occurs in an intermediate which contains 96% of the native far-UV CD signal and 80% of the native fluorescence signal. Analysis of the unfolded protein with all its prolines in the native conformation shows the existence of a very stable intermediate in the folding reaction. Mutation of a hyperexposed hydrophobic residue, Phe14, to Asn results in an increase in the free energy of unfolding of the protein of approximately 3 kcal mol-1. Kinetic analysis of the unfolding and refolding reactions of this mutant indicates that the major stabilization effect comes from the relative destabilization of the unfolded state and the kinetic intermediate with respect to the transition state, providing kinetic evidence for the inverse hydrophobic effect. This could also indicate the existence of nonnative interactions in folding intermediates.

Bacterial Proteins↗

PubMed1997

Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine.

Dihydrodipicolinate synthase (DHDPS) catalyzes the formation of dihydrodipicolinate from pyruvate and L-aspartate beta-semialdehyde (ASA). A parallel initial velocity pattern that displays competitive substrate inhibition by ASA and dead-end inhibition patterns obtained at pH 8 are consistent with a ping pong kinetic mechanism for DHDPS. The results suggest that pyruvate binds to free enzyme with subsequent formation of a Schiff base with an enzymic lysine residue followed by binding of ASA to the F enzyme form to initiate the second half-reaction. At low pH (5.7) the initial velocity and dead-end inhibition patterns are consistent with a sequential steady state ordered kinetic mechanism with pyruvate binding to enzyme prior to ASA. The irreversible step in the reaction, leading to the ping pong kinetic mechanism at high pH, is proposed to be loss of a proton from the methyl group of pyruvate in Schiff base with enzyme to form an enamine intermediate. Consistent with this proposal is the change to a sequential steady state ordered kinetic mechanism at low pH at or below the pK of the enamine intermediate. L-Lysine is an allosteric inhibitor of the DHDPS reaction that causes partial inhibition (approximately 90%) at saturating concentrations. Inhibition patterns for L-lysine vs pyruvate and ASA suggest that lysine binds to the F enzyme form at pH 8 with a Ki value of about 0.3 mM. An examination of the effects of different L-lysine concentrations on the kinetic parameters V/Kpyruvate, V/KASA, and V indicate that L-lysine decreases only the values of V/KASA and Vmax, which is consistent with the inhibitory effects of lysine manifested on the second half-reaction. In contrast at low pH the data suggest L-lysine binds to free enzyme with an inhibition constant of about 5 mM.

Allosteric Regulation↗

PubMed1997

Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model.

The kinetics of the helix<==>coil transition of an alanine-based peptide following a laser-induced temperature jump were monitored by the fluorescence of an N-terminal probe, 4-(methylamino)benzoic acid (MABA). This probe forms a peptide hydrogen bond to the helix backbone, which changes its fluorescence quantum yield. The MABA fluorescence intensity decreases in a single exponential relaxation, with relaxation times that are weakly temperature dependent, exhibiting a maximum value of approximately 20 ns near the midpoint of the melting transition. We have developed a new model, the kinetic version of the equilibrium 'zipper' model for helix<==>coil transitions to explain these results. In this 'kinetic zipper' model, an enormous reduction in the number of possible species results from the assumption that each molecule contains either no helical residues or a single contiguous region of helix (the single-sequence approximation). The decay of the fraction of N-terminal residues that are helical, calculated from numerical solutions of the kinetic equations which describe the model, can be approximately described by two exponential relaxations having comparable amplitudes. The shorter relaxation time results from rapid unzipping (and zipping) of the helix ends in response to the temperature jump, while the longer relaxation time results from equilibration of helix-containing and non-helix-containing structures by passage over the nucleation free energy barrier. The decay of the average helix content is dominated by the slower process. The model therefore explains the experimental observation that relaxation for the N-terminal fluorescent probe is approximately 8-fold faster than that for the infrared probe of Williams et al. [(1996) Biochemistry 35, 691-697], which measures the average helix content, but does not account for the absence of observable amplitude for the slow relaxation in the fluorescence experiments (<10% slow phase). If we assume that the activation barrier for the coil-->helix rate is purely entropic, the model can also explain the maximum in the temperature dependence of the relaxation time for the fluorescent probe. Parameters that best reproduce the melting curves and the ratio of relaxation times predict a value of the cooperativity parameter sigma which is approximately 3-fold larger than previously reported values obtained from fitting equilibrium data only. The helix growth rate of approximately 10(8) s-1 that reproduces the experimental relaxation times is approximately 100-fold slower than those observed in molecular dynamics simulations. These parameters can be used to simulate the kinetically cooperative formation of a helix from the all-coil state.

Alanine↗

PubMed2004

Measurement of enzyme kinetics using microscale steady-state kinetic analysis.

This paper describes a new technique--microscale steady-state kinetic analysis (microSKA)--that enables the rapid and parallel analysis of enzyme kinetics. Rather than physically defining a microscopic reactor through microfabrication, we show how the relative rates of reaction and transport in a macroscopic flow chamber, where the enzyme is immobilized on one wall of the chamber, results in the confinement of an enzyme-catalyzed reaction to a microscopic reactor volume adjacent to this wall. This volume has linear dimensions that are orders of magnitude smaller than the physical dimensions of the system (i.e., micrometer vs millimeter). Conversion within this volume is monitored at steady state as a function of position, rather than time. In this way, limitations due to reactor dead time and mixing are avoided. We use microSKA to determine kinetic parameters for the alkaline phosphatase-catalyzed de-phosphorylation of nonfluorescent methylumbelliferyl phosphate (MUP) to fluorescent 7-hydroxy-4-methylcoumarin (HMC) at two different values of pH. Kinetic parameters measured with microSKA are in good agreement with values obtained using conventional methods, if one takes into account effects of immobilization on enzyme activity. This technique provides a rapid and simple method for determining enzyme kinetics using small amounts of sample material and may be useful for applications in proteomics, drug discovery, biocatalyst development, and clinical diagnostics.

Alkaline Phosphatase↗

PubMed1997

Kinetics of low-density lipoprotein receptor activity in Hep-G2 cells: derivation and validation of a Briggs-Haldane-based kinetic model for evaluating receptor-mediated endocytotic processes in which receptors recycle.

The process of receptor-mediated endocytosis for receptors that recycle to the cell surface in an active form can be considered as being kinetically analogous to that of a uni-substrate, uni-product enzyme-catalysed reaction. In this study we have derived steady-state initial-velocity rate equations for this process, based on classical Briggs-Haldane and King-Altman kinetic approaches to multi-step reactions, and have evaluated this kinetic paradigm, using as a model system the low-density lipoprotein (LDL)-receptor-mediated endocytosis of the trapped label [14C]sucrose-LDL in uninduced, steady-state Hep-G2 cells. Using the derived rate equations, together with experimentally determined values for Bmax (123 fmol/mg of cell protein), Kd (14.3 nM), the endocytotic rate constant ke (analogous to kcat; 0.163 min-1), Km (80 nM) and maximal internalization velocity (26.4 fmol/min per mg), we have calculated the ratio ke/Km (0.00204 nM-1.min-1), the bimolecular rate constant for LDL and LDL-receptor association (0. 00248 nM-1.min-1), the first-order rate constant for LDL-LDL-receptor complex dissociation (0.0354 min-1), the total cellular content of LDL receptors (154 fmol/mg of cell protein), the intracellular LDL receptor concentration (30.7 fmol/mg of cell protein) and the pseudo-first-order rate constant for LDL receptor recycling (0.0653 min-1). Based on this mathematical model, the kinetic mechanism for the receptor-mediated endocytosis of [14C]sucrose-LDL by steady-state Hep-G2 cells is one of constitutive endocytosis via independent internalization sites that follows steady-state Briggs-Haldane kinetics, such that LDL-LDL-receptor interactions are characterized by a rapid-high-affinity ligand-receptor association, followed by ligand-receptor complex internalization that is rapid relative to complex dissociation, and by receptor recycling that is more rapid than complex internalization and that serves to maintain 80% of cellular LDL receptors on the cell surface in the steady-state. The consistency with which these quantitative observations parallel previous qualitative observations regarding LDL-receptor-mediated endocytosis, together with the high correlation between theoretical internalization velocities (calculated from determined rate constants) and experimental internalization velocities, underscore the validity of considering receptor-mediated endocytotic processes for recycling receptors in catalytic terms.

Carcinoma, Hepatocellular↗

PubMed1983

Delayed kinetics of VO2 in the transition from prior exercise. Evidence for O2 transport limitation of VO2 kinetics: a review.

The influence of prior exercise state on the kinetics of VO2, VE, and HR was studied in six subjects. The exercise conditions tested were square wave increases in work rate from rest to 80% of the work rate at anaerobic threshold (AT), from O W loadless pedaling to 80% AT, from rest to 40% AT, and from 40% to 80% AT. The kinetic response was evaluated by the time constant (tau) and mean response time (MRT = time to achieve 63% response) as determined by nonlinear regression. For both VO2 and HR, tau and MRT were not significantly different in the rest or O W to 80% AT tests, but were significantly faster in the rest to 40% AT test and significantly slower in the 40% to 80% AT test than the rest and O W to 80% AT tests. The tau for VE was significantly slower in the 40% to 80% AT tests than in the other tests. The coincident variation of HR and VO2 kinetics is taken as support for the hypothesis that VO2 kinetics are controlled by oxygen transport. Evidence from the literature that supports both the oxygen transport and the oxygen utilization for the control of VO2 kinetics is reviewed.

Adult↗

PubMed2004

Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain.

Because of the association of beta-sheet formation with the initiation and propagation of amyloid diseases, model systems have been sought to further our understanding of this process. WW domains have been proposed as one such model system. Whereas the folding of the WW domains from human Yes-associated protein (YAP) and Pin have been shown to obey single-exponential kinetics, the folding of the WW domain from formin-binding protein (FBP) 28 has been shown to proceed via biphasic kinetics. From an analysis of free-energy landscapes from atomic-level molecular dynamics simulations, the biphasic folding kinetics observed in the FBP WW domain may be traced to the ability of this WW domain to adopt two slightly different forms of packing in its hydrophobic core. This conformational change is propagated along the peptide backbone and affects the position of a tryptophan residue shown in other WW domains to play a key role in binding. The WW domains of Pin and YAP do not support more than one type of packing each, leading to monophasic folding kinetics. The ability of the FBP WW domain to assume two different types of packing may, in turn, explain the capacity of this WW domain to bind two classes of ligand, a property that is not shared by other WW domains. These findings lead to the hypothesis that lability with respect to conformations separated by an observable barrier as a requirement for function is incompatible with the ability of a protein to fold via single-exponential kinetics.

Adaptor Proteins, Signal Transducing↗

PubMed1997

D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. I. Kinetic mechanism and pH dependence of kinetic parameters, coenzyme binding and substrate inhibition.

The steady-state kinetics of D-2-hydroxy-4-methylvalerate dehydrogenase have been studied at pH 8.0 by initial velocity, product inhibition, and dead-end inhibition techniques. The mechanism is rapid-equilibrium ordered in the NAD+ plus D-2-hydroxy-4-methylvalerate direction, and steady-state ordered in the other direction. In both cases coenzyme is the first substrate added and both the E-NADH-D-2-hydroxy-4-methylvalerate and E-NAD+-2-oxo-4-methylvalerate give rise to abortive complexes which cause excess substrate inhibition. Steady-state measurements show that the rate-limiting step in both directions at pH 8.0 is between formation of the enzyme-coenzyme-substrate ternary complex and the release of the first product of the reaction. Transient kinetics combined with primary kinetic deuterium isotope effects show that in the NADH-->NAD+ direction there is a slow, rate-limiting rearrangement of the E-NADH-oxoacid complex while hydride transfer is very fast. The release of NAD+ at pH 8.0 is 200-times faster than Kcat (NADH-->NAD+) whereas the release of NADH is only 5-times faster than Kcat (NAD+-->NADH). The pH dependence of NADH binding depends upon the presence of two ionizable residues with a pKa of about 5.9. The pH dependence of kinetic parameters is explained by a third ionizable residue with pKa values 7.2 (in the E-NADH complex) and < or = 6.4 (in the E-NAD+ complex) which may be the proton donor and acceptor for the chemical reaction. At pH 6.5 the mechanism changes in the NADH-->NAD+ direction to be partly limited by the chemical step with a measured primary kinetic isotope effect of 5.7 and partly by an only slightly faster dissociation of NAD+. In addition the inhibition by excess oxo-4-methylvalerate is more pronounced. The mechanism implies that removing the positive charges created by the two groups which control coenzyme affinity could both enhance the catalytic rate at pH 6.5 and diminish excess substrate inhibition to provide an enzyme better suited to the bulk synthesis of D-2-hydroxyacids.

Alcohol Oxidoreductases↗

PubMed2003

Isoform selectivity and kinetics of morphine 3- and 6-glucuronidation by human udp-glucuronosyltransferases: evidence for atypical glucuronidation kinetics by UGT2B7.

Morphine elimination involves UDP-glucuronosyltransferase (UGT) catalyzed conjugation with glucuronic acid to form morphine 3- and 6-glucuronides (M3G and M6G, respectively). It has been proposed that UGT2B7 is the major enzyme involved in these reactions, but there is evidence to suggest that other isoforms also catalyze morphine glucuronidation in man. Thus, we have characterized the selectivity and kinetics of M3G and M6G formation by recombinant human UGTs. UGT 1A1, 1A3, 1A6, 1A8, 1A9, 1A10, and 2B7 all catalyzed M3G formation, but only UGT2B7 formed M6G. The kinetics of M3G formation by the UGT1A family isoforms was consistent with a single enzyme Michaelis-Menten model, with apparent Km values ranging from 2.6 to 37.4 mM. In contrast, M3G and M6G formation by UGT2B7 exhibited atypical kinetics. The atypical kinetics may be described by a model with high- and low-affinity Km values (0.42 and 8.3 mM for M3G, and 0.97 and 7.4 mM for M6G) from fitting to a biphasic Michaelis-Menten model. However, a multisite model with an interaction between two identical binding sites in a negative cooperative manner provides a more realistic approach to modeling these data. According to this model, the respective binding affinities (Ks) for M3G and M6G were 1.76 and 1.41 mM, respectively. These data suggest that M6G formation may be used as a selective probe for UGT2B7 activity, and morphine glucuronidation by UGT2B7 appears to involve the simultaneous binding of two substrate molecules, highlighting the need for careful analysis of morphine glucuronidation kinetics in vitro.

Cell Line↗

PubMed1991

In vivo dissociation kinetics of [3H]quinuclidinyl benzilate: relationship to muscarinic receptor concentration and in vitro kinetics.

The in vivo washout kinetics of [3H]quinuclidinyl benzilate ([3H]QNB) varies significantly in various structures in the rat brain. The slowest washout rates are from the hippocampus, corpus striatum, and cortex, intermediate rates are exhibited from the thalamus and colliculi, while the fastest washout rate is from the cerebellum. We have also demonstrated a difference in the in vitro dissociation rates (k-1) of [3H]QNB from various structures. The k-1 for the hippocampus, corpus striatum and cortex, is two-fold slower than that observed in the thalamus, colliculi, and cerebellum. The differences in the in vitro dissociation kinetics are not, however, sufficient to explain the differences in the in vivo washout kinetics. We have developed a theoretical formulation which describes conditions under which the washout kinetics are a function of the concentration of receptor in a structure. Furthermore, we present a graphical method in which a plot of the reciprocal of the observed washout rate constant, 1/k(obs), vs receptor concentration is linear. Analysis of the washout kinetics of [3H]QNB from various structures of the CNS of rat were well described by this theory when the differences in in vitro k-1 are included.

Animals↗

PubMed2002

Simulation of trichloroacetic acid kinetics in the isolated perfused rat liver using a biologically based kinetic model.

Trichloroacetic acid (TCA) is a contaminant of drinking water. It induces peroxisome proliferation in livers of rats and mice and is hepatocarcinogenic in the latter species. Previous experimental studies of the kinetics of TCA in the isolated perfused rat liver (IPRL) at two doses have been reported. To gain more insight into the mechanistic processes controlling TCA kinetics in the liver a biologically based kinetic (BBK) model for the IPRL was used to analyze the experimental data. The IPRL was exposed to 25, 250, or 1000 microM TCA for 2 h in a recirculating perfusion system. These doses were not cytotoxic. The BBK model simulated the TCA concentration in perfusion medium and liver, and the biliary excretion of TCA. Separate protein binding studies showed that over 90% of TCA was bound to albumin in the perfusion medium whereas binding in liver homogenate was much lower. Integrating the information on protein binding into the BBK model, the hepatic uptake of TCA and its biliary excretion could be fitted assuming asymmetrical saturable transport at the sinusoidal membrane and linear transport at the bile canalicular membrane. To validate the BBK model, additional washout experiments were conducted in which the perfusion medium was replaced with TCA-free medium after 30 min of exposure of the liver to 1000 microM TCA. This approach illustrates the usefulness of BBK modeling for analyzing experimental kinetic data and gaining insight in kinetic mechanisms controlling the behavior of a chemical in the liver.

Animals↗

PubMed2001

Pre-steady-state kinetics of initiation of transcription by T7 RNA polymerase: a new kinetic model.

In order to begin to understand the mechanism of the initiation of transcription in the model bacteriophage T7 RNA polymerase system, the simplest possible reaction, the synthesis of a dinucleotide, has been followed by quench-flow kinetics and numerical integration of mechanism-specific rate equations has been used to test specific kinetic models. In order to fit the observed time dependence in the pre-steady-state kinetics, a model for dinucleotide synthesis is proposed in which rebinding of the dinucleotide to the enzyme-DNA complex must be included. Separate reactions using dinucleotide as a substrate confirm this mechanism and the determined rate constants. The dinucleotide rebinding observed as inhibition under these conditions forms a productive intermediate in the synthesis of longer transcripts, and must be included in future kinetic mechanisms. The rate-limiting step leading to product formation shows a substrate dependence consistent with the binding of two substrate GTP molecules, and at saturating levels of GTP, is comparable in magnitude to the product release rate. The rate of product release shows a positive correlation with the concentration of GTP, suggesting that the reaction shows base-specific substrate activation. The binding of another substrate molecule, presumably via interaction with the triphosphate binding site, likely facilitates displacement of the dinucleotide product from the complex.

Bacteriophage T7↗

PubMed1985

Kinetics of (Na+ + K+)-ATPase: analysis of the influence of Na+ and K+ by steady-state kinetics.

The influence of Na+ and K+ on the steady-state kinetics at 37 degrees C of (Na+ + K+)-ATPase was investigated. From an analysis of the dependence of slopes and intercepts (from double-reciprocal plots or from Hanes plots) of the primary data on Na+ and K+ concentrations a detailed model for the interaction of the cations with the individual steps in the mechanism may be inferred and a set of intrinsic (i.e. cation independent) rate constants and cation dissociation constants are obtained. A comparison of the rate constants with those obtained from an analogous analysis of Na+-ATPase kinetics (preceding paper) provides evidence that the ATP hydrolysis proceeds through a series of intermediates, all of which are kinetically different from those responsible for the Na+-ATPase activity. The complete model for the enzyme thus involves two distinct, but doubly connected, hydrolysis cycles. The model derived for (Na+ + K+)-ATPase has the following properties: The empty, substrate free, enzyme form is the K+-bound form E2K. Na+ (Kd = 9 mM) and MgATP (Kd = 0.48 mM), in that order, must be bound to it in order to effect K+ release. Thus Na+ and K+ are simultaneously present on the enzyme in part of the reaction cycle. Each enzyme unit has three equivalent and independent Na+ sites. K+ binding to high-affinity sites (Kd = 1.4 mM) on the presumed phosphorylated intermediate is preceded by release of Na+ from low-affinity sites (Kd = 430 mM). The stoichiometry is variable, and may be Na:K:ATP = 3:2:1. To the extent that the transport properties of the enzyme are reflected in the kinetic ATPase model, these properties are in accord with one of the models shown by Sachs ((1980) J. Physiol. 302, 219-240) to give a quantitative fit of transport data for red blood cells.

Binding Sites↗

PubMed1980

Adaptation of the EMIT theophylline assay to kinetic analyzers: the relationship of reaction kinetics to calculation procedures.

We investigated the kinetic characteristics of an enzyme immunoassay system (EMIT) for the determination of theophylline. Less than 10% of the glucose-6-phosphate and NAD+ are consumed and the glucose-6-P-dehydrogenase-theophylline complex is essentially saturated with these substrates during the course of the reaction. However, apparently as the result of antibody heterogeneity, the rate does change during the course of the reaction. As a result, the values of the kinetic parameters for the theophylline saturation curve vary with the timing interval chosen for measurement. We show that the values of these parameters govern the application of the available methods of calculating EMIT data, the graphical procedure suggested by the manufacturer, logit-log, log-log, and curve fitting. These studies (1) explain the basis of the graphical procedure and why it does not always provide proper calibration, (2) show that to appropriately understand the application of any of the calculation procedures one should determine the values of the kinetic constants of the theophylline saturation curve in the particular assay conditions, and (3) illustrate simple, practical procedures for determining the values of these constants for any instrument-EMIT assay system. Specific illustrations are shown for the EMIT theophylline system with two kinetic analyzers, the Abbott ABA-100 and Gilford 3500, with which markedly different reaction conditions are used.

Autoanalysis↗

PubMed1982

The sodium currents of nerve under voltage clamp as heterogeneous kinetics. A model that is consistent with possible kinetic behavior.

A model is presented which explains in Na+ currents of voltage-clamped nerve as resulting from a heterogeneous initiation of a sequential kinetic process. This is in analogy with the heterogeneity of the kinetics of other dielectric relaxations. The results suggest that: (1) The kinetic processes responsible for the voltage response occur within the membrane rather than at the surface; (2) The heterogeneity is due to simultaneous thermal diffusion and electric field-induced charge migration: (3) The slow turnoff upon prolonged depolarization is a voltage-independent, thermally controlled process; (4) The fast turnoff upon instantaneous repolarization is the reverse of the turning-on process. All the kinetic parameters depend on the transmembrane potential in accord with the possible behavior expected from activated-state theory. The diffusion coefficient of the charged species in the membrane as found from the data agrees with that found by photobleaching experiments on general proteins in membranes. The charge on the molecule responsible for the heterogeneous "gating' can be calculated unambiguously from the data.

Electric Conductivity↗

PubMed1988

Glucose-6-phosphate dehydrogenase from Dicentrarchus labrax liver: kinetic mechanism and kinetics of NADPH inhibition.

The kinetic mechanism of the reaction catalyzed by glucose-6-phosphate dehydrogenase (EC 1.1.1.49) from Dicentrarchus labrax liver was examined using initial velocity studies, NADPH and glucosamine 6-phosphate inhibition and alternate coenzyme experiments. The results are consistent with a steady-state ordered sequential mechanism in which NADP+ binds first to the enzyme and NADPH is released last. Replots of NADPH inhibition show an uncommon parabolic pattern for this enzyme that has not been previously described. A kinetic model is proposed in agreement with our kinetic results and with previously published structural studies (Bautista et al. (1988) Biochem. Soc. Trans. 16, 903-904). The kinetic mechanism presented provides a possible explanation for the regulation of the enzyme by the [NADPH]/[NADP+] ratio.

Animals↗

PubMed2005

A respirometric method for characterising the organic composition and biodegradation kinetics and the temperature influence on the biodegradation kinetics, for a mixture of sludge and bulking agent to be co-composted.

A respirometric method was set up to study kinetics of biological reactions involved in the treatment of organic wastes-sludge mixed with pine barks--by composting. Oxygen consumption rates of this type of mixture were monitored during 10-20 days, using a 10 l respirometric cell kept at constant temperature and moisture. Oxygen consumption kinetics were modelled and organic matter composition was characterised as biomass, easily-biodegradable, slowly-biodegradable and non-biodegradable organic matter. The influence of temperature on kinetics was tested. Results show that this respirometric method is a useful tool for the characterisation of solid organic matter biodegradability and for the modelling of the biological kinetics of the composting process.

Biodegradation, Environmental↗

PubMed2006

Experimental and theoretical studies of sorption kinetics of the anthracycline antitumor antibiotic rubomycin on a carboxylic heterogeneous sorbent. Bidisperse model of sorption kinetics.

The present work is devoted to experimental and theoretical studies of the sorption kinetics of the anthracycline antitumor antibiotic rubomycin on a carboxylic heteroreticular sorbent, BDM-12. The dependence of sorption kinetic parameters on the radius of sorbent grains has been experimentally obtained. The comparison of experimental data with the predictions of both homogeneous and "shell-and-core" models demonstrates the impossibility of using these models for adequate description of the rubomycin sorption kinetics on the sorbent, BDM-12. We have proposed a theory using the bidisperse model of heterogeneous sorbent grain and "linear driving force" approximation. This approximation can be applied at 10(-3) < alpha = tauI/tauA < 1, x < 1 and gives the values of the degree of process completion with relative errors approximately (alpha x)2. Here tauI and tauA are the characteristic times required for diffusion penetration into the macro- and microspheres, respectively, x is the ratio of the microsphere and macrosphere uptakes at equilibrium. The dependences of two characteristic times of the sorption process (for short- and long-time regions) on the radius of a sorbent grain have been derived. The predictions of the theory developed here are in good agreement with our experimental data and make it possible to calculate the kinetic parameters tauI, tauA and x.

Adsorption↗