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Time course of glucose binding by histone HI and total histones was followed in isolated histone preparations and in thymus nuclei. In both cases the uptake of glucose by HI was surprisingly high in contrast to a much lower uptake of glucose by total histones. DNA is not implicated in glycation of histones in nuclei.
In this paper we present the results of studies on the influence of an initial substrate concentration (NO3-, sodium lactate) on the kinetics of denitrification. We have found that the optimum rates of the process are obtained at 37°C for the nutrient medium containing sodium lactate at a concentration of 2.52 g/dm3, and nitrate nitrogen 1,4 g/dm3.
Kinetics of the reaction of peroxynitrite with ferric cytochrome c in the absence and presence of bicarbonate was studied. It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. The rates of the absorbance changes in the Soret region of cytochrome c spectrum caused by peroxynitrite or peroxynitrite/bicarbonate were the same as the rate of spontaneous isomerization of peroxynitrite or as the rate of the reaction of peroxynitrite with bicarbonate, respec­tively. This means that intermediate products of peroxynitrite decomposition, OH/ NO2 or, in the presence of bicarbonate, CO3- / NO2, are the species responsible for the absorbance changes in the Soret band of cytochrome c. Modifications of the heme center of cytochrome c by radiolytically produced radicals, OH, NO2 or CO3- , were also studied. The absorbance changes in the Soret band caused by radiolytically produced OH or CO3- were much more significant that those observed after peroxy­nitrite treatment, compared under similar concentrations of radicals. NO2 produced radiolytically did not interact with the heme center of cytochrome c. Cytochrome c ex­hibited an increased peroxidase-like activity after reaction with peroxynitrite as well as with radiolytically produced OH, NO2 or CO3- radicals. This means that modifi­cation of protein structure: oxidation of amino acids and/or tyrosine nitration, facili­tates reaction of H2O2 with the heme iron of cytochrome c, followed by reaction with the second substrate.
In the open transcription complex (RPo), Escherichia coli RNA polymerase o and a70 subunits are known to be in contact with each other and with the promoter region overlapping the -35 hexamer and the proximal part of the UP element. To probe the effect of An DNA bending tracts in this region on initiation of transcription, kinetics of the formation of RPo by Escherichia coli RNA polymerase at two groups of synthetic consensus-like promoters bearing single DNA bending tracts (i) A5 within the proxi­mal subsite region of the UP element (promoters Pk and Pl) and (ii) A5 (Pg) or A8 (Pm) in the region including the downstream end of the proximal UP subsite and the -35 consensus hexamer was studied in vitro using the fluorescence-detected abortive initi­ation assay. The kinetic data obtained demonstrate that the overall second-order rate constant ka of RPo formation is: (i) by almost one order of magnitude larger at Pk and Pl, relative to that at a control unbent promoter, and mainly due to a higher value of the equilibrium constant, Kj, of the initial closed complex; and (ii) several-fold smaller at Pg and Pm owing to a strongly decreased value of K^. For Pm, the latter parameter was found to be dependent exponentially on four Mg ions, as compared with the seven ions remaining in equilibrium with the initial closed complex at the parent Pa promoter. This indicates that promoter region bearing a stiff A8 T8 fragment of B'-DNA forms a smaller number of ionic contacts with the a subunit. These findings provide a new insight to and support the present model of interactions between RNA polymerase a and o subunits with the proximal UP subsite and the -35 region of pro­moters.
The aim of this study was to verify first-order kinetic reaction rate model performance in predicting of leaching of atrazine and inorganic compounds (K+1, Fe+3, Mg+2, Mn+2, NH4 +, NO3 - and PO4 -3) from tilled and orchard silty loam soils. This model provided an excellent fit to the experimental concentration changes of the compounds vs. time data during leaching. Calculated values of the first-order reaction rate constants for the changes of all chemicals were from 3.8 to 19.0 times higher in orchard than in tilled soil. Higher first-order reaction constants for orchard than tilled soil correspond with both higher total porosity and contribution of biological pores in the former. The first order reaction constants for the leaching of chemical compounds enables prediction of the actual compound concentration and the interactions between compound and soil as affected by management system. The study demonstrates the effectiveness of simultaneous chemical and physical analyses as a tool for the understanding of leaching in variously managed soils.
Приведены результаты исследования кинетики распределения водорода в сварном соединении в зависимости от температурных режимов.
Biosorption is an attractive technology which is used for the sorption of substances by a biomaterial. In this present work the heavy metal chromium was subjected to biosorption because of their non-degradability nature and causes water and land pollution. Cherry leaves were used as a biomaterial for the biosorption. Kinetic studies were performed for the biosorption experiment. From the experiment it was found that the reaction follows pseudo first order reaction because of the larger value of regression coefficient R2 and lower value of standard errors (χ2) for pseudo first order reaction than second order reaction.
A single pyrimidine nucleoside phosphorylase was found in the cytoplasmic extract from Hymenolepis diminuta. This enzyme preferentially cleaves uridine and, to a much lesser extent, thymidine. Its presence directly indicates the existence of pyrimidine nucleoside salvage pathway in this parasite. Detailed kinetic studies in the phosphorolytic and synthetic direction pointed to the sequential mechanism of these reactions. For phosphorolysis, Kurd = 33 ^M and Kp = 806 nM. For synthesis of uridine, KUra = 204 jiM and Ki.p.rib.= 50 pM. Over six times higher Km for uracil than for uridine indicates that phosphorolysis is the favoured reaction in this tapeworm. Well known inhibitors of mammalian uridine phosphorylase: 2,2'-anhydro-5- -ethyluridine and l-(l,3-dihydroxy-2-propoxymethyl)-5-benzyluracil (DHPBU), both with Ki = 0.07 nM were potent competitive inhibitors of the enzyme from H. diminuta. The newly synthesized 2,3'-anhydro-5-ethyluridine (K. Felczak,unpublished) showed only moderate inhibitory activity (Ki = 14 jiM) similarly as l-(l,3-dihydroxy-2- -propoxy-methyl)-5-benzyluracil. The same order of Ki values obtained for the investigated inhibitors vs uridine phosphorylase, irrespective whether the enzyme was isolated from rat intestinal mucosa (Drabikowska etal., 1987,Biochem. Pharmacol. 36,4125-4128) or H. diminuta may point to a great similarity between binding sites on the parasite and the host enzyme.
In this paper we present the results of the study on the effect of n-decane, n-pentane, diesel oil and petrol on the denitrifieation process occuring in the presence of Bacillus licheniformis bacteria. We found that only diesel oil and n-decane could be degraded during denitrifieation catalyzed by bacteria, while petrol and n-pentane inhibited the process.
In this paper the effect of Mo6+, W6+, and Cu2+ ions on kinetics of denitrification and growth of Bacillus licheniformis is presented. The absence lack of Mo6+ and Cu2+ in the growth medium appeared to have no effect on the kinetics of the process. This fact suggests that these ions are not a part of the active centers of denitrification enzymes. Additionaly tungsten (VI) which is competitive to molybdenum (VI) does not inhibit denitrification in concentrations up to 0.1 g/dm3. Molibdenum (VI) starts to inhibit denitrification from 5.0 g/dm3 and copper (II) starting from 0.03 g/dm3.
Kinetics of the smooth muscle calponin-F-actin interaction was studied by stopped- flow measurements of light scattering and fluorescence intensity of pyrene-labelled F-actin. The intensity and character of the changes in light scattering, and thus the mode of calponin binding to actin filaments leading to changes in their shape and bun­dling, depend on the molar ratio of the two proteins. Parallel measurements of pyrene-fluorescence quenching upon calponin binding revealed that intrinsic conformational changes in actin filaments are delayed relative to the binding process and are not markedly influenced by the mode of calponin binding. Bundling of actin filaments by calponin was not correlated with fluorescence changes and thus with al­terations in the structure of actin filaments.
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