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PL
Przebadano charakterystykę albumin surowicy bydlęcej BSA (bovine serum albumin) poddanych działaniu trzech dienoaldehydów (trans, trans-2,4-heptadienal, trans,trans-2,4-nonadienal i trans,trans-2,4-dekadienal). Utrata grupy aminowej i zwiększenie liczby karbonylowej wskazywały na uszkodzenie łańcucha bocznego BSA. Wyniki elektroforezy przeprowadzonej z wykorzystaniem żelu dodecylosiarczan sodu-poliakryloamid wskazały, że wszystkie stosowane aldehydy doprowadziły do powstania agregatów BSA, przy czym najbardziej znaczący efekt zaobserwowano dla heptadienalu. Zmiany wewnętrznej fluorescencji i hydrofobowości powierzchni BSA wskazywały, że aldehydy zmodyfikowały białkową strukturę BSA. Spowodowały ponadto, że albuminy BSA utworzyły żółtobrązowe addukty i fluorescencyjną lipofuscynę. Addukty heptadienal-BSA wykazywały zwiększoną absorbancję w zakresie UV-Vis 270-280 nm oraz 300-400 nm, podobnie jak oba pozostałe addukty aldehyd-BSA. Zaobserwowano silne korelacje między tworzeniem się grup karbonylowych połączonych z białkami, współczynnikiem retencji zawartości wolnych grup aminowych oraz maksymalną wartością absorpcji UV-Vis a zawartością aldehydów. Przeprowadzono także analizę składu podstawowych produktów utleniania i dokonano oceny wpływu parametrów utleniania na modyfikację BSA. Zaobserwowano większe uszkodzenie BSA podczas działania krótkołańcuchowych aldehydów zastosowanych w większych stężeniach.
EN
Bovine serum albumin (BSA) was incubated with trans, trans-2,4-heptadienal, trans,trans-2,4-nonadienal, and trans, trans-2,4-decadienal (concns. 1-50 mM) at 37°C for 24 h to produce yellowish-brown adducts and fluorescent lipofuscin. Loss of the amino groups and increased carbonyl value of the product were indicative for BSA side chain damage. The Na dodecyl sulfate-polyacrylamide gel electrophoresis showed the aggregation of BSA. Changes in intrinsic fluorescence and surface hydrophobicity value of BSA indicated the modification of protein structure. The heptadienal-BSA adducts exhibited an increased UV-Vis absorbance at 270-280 nm and 300-400 nm, similarly to the 2 other aldehyde-BSA adducts. Strong correlations were obsd. between formation of protein-bound carbonyls, the retention ratio of free amino content, max. UV-Vis absorption value, and concn. of aldehydes. Principal component anal. was also performed. In general, the BSA damage increased with increasing the aldehyde concn. and decreasing their chain length.
EN
Purpose: This study focuses on increasing production of biogas as an alternative energy from biodegradable wastes (BWs) using BSA coated iron oxides nanoparticles, in view of solving waste management at household level. Many attempts have been performed in order to increase biogas production, including thermal pre-treatment of organic waste, but all of them present limited industrial applications. Iron has been shown to enhance anaerobic digestion, but there are severe drawbacks for introducing the metal ion in an anaerobic closed reactor. Design/methodology/approach: Process for the production of biogas from biodegradable material which comprises the steps of: (a) adding the biodegradable material to the Bio- reactor,(b) inoculating the microorganisms in the digester,(c) synthesis iron oxides and BSA powder coated on the particles (d) adding a colloidal solution of surface-modified BSA-iron oxide nanoparticles to the reactor; (e) providing anaerobic conditions; (f) carrying out the anaerobic digestion; and (g) collecting the biogas, wherein the steps (a), (b) and (c) can be carried out in any order. It also comprises the use of BSA-iron oxide nanoparticles capable of supplying Fe ions to the media for biogas production in anaerobic conditions and in the presence of Fe ions in the media.
PL
Chemiczna modyfikacja struktury barwników skwaryliowych daje nowe układy chromoforowe o szerokim zakresie właściwości optycznych, takich jak absorpcja światła i emisja fluorescencji, z zakresu światła od widzialnego do bliskiej podczerwieni. Otrzymano nowe funkcjonalne barwniki, w których pod wpływem bodźca zewnętrznego lub oddziaływań chemicznych, zachodzą zmiany w rozmieszczeniu ładunku elektronowego w chromoforze skwaryliowym. Z uwagi na wyraźne zmiany ich właściwości spektroskopowych pod wpływem połączenia z substancją analizowaną, mogą zaleźć praktyczne zastosowanie, jako markery fluorescencyjne do oznaczania biocząsteczek.
EN
Chemical modification of the structure of squarylium dyes gives a new chromophoric systems that have a wide range of optical properties, such as the light absorption and fluorescence emission in the range from the visible light to the near infrared one. The new functional dyes in which the changes of the electron charge distribution in chromophore under the influence of an external stimulus or chemical undergo have been obtained. The interaction between dye and analyte leads to the significant changes of their spectroscopic properties. It can give the possibility of practical application of these new dyes as the fluorescent markers for biomolecules labeling.
EN
The binary and ternary complex formations of poly(methyl vinyl ether-co-maleic anhydride) (PMVEMA) with copper ions and with bovine serum albumin (BSA) in the presence of copper ions in phosphate buffer solution at pH = 7 were examined by the techniques of UV-visible, fluorescence, dynamic light scattering, atomic force microscopy measurements. In the formation of binary complexes of PMVEMA-Cu(II), the addition of copper ions to the solution of PMVEMA in phosphate buffer solution at pH = 7 forms homogeneous solutions when the molar ratio of Cu(II)/MVEMA is 0.5. Then the formations of ternary complexes of PMVEMA-Cu(II)-BSA were examined. Study analysis revealed that the toxicities of polymer-metal and polymer-metal-protein mixture solutions depend on the nature and ratio of components in mixtures.
EN
The results of ultrafiltration tests carried out in a cross-flow mode with BSA model solutions using a laboratory scale setup equipped with fiat ceramic membranes are presented. The influence of operating parameters such as TMP, NaCl concentration and pH on membrane permeability was investigated. A decline in permeate flux with the increase of TMP and NaCl concentration and the decrease of pH was observed during tests. Membrane permeability for pure water was found in order to determine the membrane resistance RM for different TMP values. A short analysis of fouling phenomenon was performed based on the calculated flux decline and fouling resistance.
PL
Przedstawiono wyniki badań ultrafiltracji w układzie krzyżowym (crossflow) modelowych roztworów BSA przy użyciu instalacji laboratoryjnej z płaskimi membranami ceramicznymi. Badano wpływ parametrów operacyjnych takich jak TMP, stężenie NaCl i pH na przepuszczalność membrany. Dla wyższych wartości TMP oraz stężenia NaCl oraz niższych wartości pH obserwowano spadek strumienia objętościowego permeatu. W celu ustalenia wielkości oporu membrany RM dla różnych wartości TMP wyznaczono przepuszczalność membrany dla wody. Przeprowadzano krótką analizę zjawiska foulingu na podstawie obliczonego spadku strumienia objętościowego permeatu oraz oporu foulingu.
EN
The results of ultrafiltration tests carried out with model BSA and myoglobin solutions using ceramic 50 and 150 kDa membranes have been presented. Membrane permeability and selectivity were investigated in function of pH, transmembrane pressure (TMP) as well as molecular modelling data for proteins such as size, geometrical parameters and pH of minimal free energy of folding. The study has shown that the permeate flux J(v) depends on TMP, whereas the protein rejection is mainly influenced by pH. The results demonstrated that molecular modelling data are not sufficient to explain the membrane behaviour and the membrane–protein charge interactions and fouling effects must be also considered to explain the rejection mechanisms.
EN
This study was motivated by the need to provide more insight into the possible mechanism of the intermolecular interactions between antispasmodic drug drotaverine and one of the serum albumins (BSA), with the aim to indicate the most probable sites of these interactions. For this purpose both experimental (spectrofluorometric titration at various temperatures) and theoretical (molecular mechanics) methods have been applied. The obtained results clearly showed that drotaverine quenched BSA fluorescence, and the most probable mechanism is static quenching. The negative value of the theoretically predicted binding free Gibbs energy (-23.8 kJ/mol) confirmed the existence of the intermolecular interactions involving drotaverine and one tryptophan within BSA protein and was well agreed with the experimentally determined value of -25.2 kJ/mol.
EN
The binding of harmane with human serum albumin (HSA) and bovine serum albumin (BSA) were studied by fluorescence and phosphorescence spectroscopic methods. Quenching of fluorescence of serum albumins by harmane was found to be a static quenching process. The equilibrium constant (K) of complex formation was found to be equal to (5.16±0.28)x104 M-1 and (4.32±0.30)x104 M-1 for HSA and BSA, respectively. It was found that the interactions of harmane with HSA and BSA were also in the excited triplet state. The determined bimolecular constant or triplet state quenching (kqT)of the proteins studied by harmane was (1.15± 0.10)x107 M-1 s-1 and (2.88±0.22)x107 M-1 s-1 for HSA and BSA, respectively. Based on the similar value of K and kqT for HSA and BSA, a possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa.
EN
A mixed complex Fe(bpy)(phen)2+ was synthesized and resonance light-scattering (RLS) characteristics of a triple complex Fe(bpy)(phen)SO4-Myristylpyridinium bromide-bovine serum albumin were studied. When albumin was added, Fe(bpy)(phen)2+-1.
PL
Otrzymano mieszany kompleks Fe(bpy)(phen) )2+ i zbadano charakterystykę rezonansowego rozpraszania światła (RLS) przez potrójny kompleks Fe(bpy(phen)SO42+ ulegał agregacji na powierzchni jej cząsteczek. W rezultacie sygnały RLS ulegały wzmocnieniu przy 400 nm i 470 nm. Intensywność sygnału RLS była proporcjonalna do stężenia albuminy wołowej. Stwierdzono, że obecność jonu mirystylopirydyniowego zwiększała czułość układu. Granicę oznaczalności określono na 0,02 mg L-1.
11
Content available remote The study of interactions between diclofenac and bovine serum albumin (BSA)
EN
Investigation of the interactions between diclofenac and BSA was performed using UV-Vis absorption and fluorescence methods. There was a quenching effect found between these two molecules in the fluorescence measurement methods; steady-state and time-resolved. The fluorescence decay time enables to determine the quenching mechanism and thus conclude that the complex is formed in ground-state but also collisional quenching - when the excited-state fluorophore of BSA is deactivated - occurs. Computer modeling was applied to observe and optimize the formation of the complex between N-acetyl-L-tryptophamide and diclofenac.
PL
W pracy zbadano oddziaływania pomiędzy diklofenakiem i surowiczą albuminą wołową przy użyciu metod spektroskopii absorpcyjnej UV-Vis oraz metod fluorescencyjnych. Wyniki wskazują na istnienie interakcji pomiędzy cząsteczkami zarówno w stanie wzbudzonym (wygaszanie dynamiczne) jak i podstawowym (powstanie niefluoryzującego kompleksu). Za pomocą modelowania molekularnego zdołano zoptymalizować kompleks pomiędzy diklofenakiem a N-acetylo-L-tryptofanamidem.
EN
The mechanism of interaction of bromocresol purple (BCP) with bovine serum albumin (BSA) has been investigated by spectrofluorometric and circular dichroism methods. Association constant for the BCP-BSA system showed that the interaction is non-covalent in nature and that there occurs only a partial occupation of a binding site. Binding studies in the presence of hydrophobic probe, 8-anilino-1-naphthalene sulphonic acid, sodium salt (ANS) showed that there is hydrophobic interaction between BCP and ANS and they may share common sites in BSA. Stern-Volmer analysis of fluorescence quenching data showed that the fraction of fluorophore (protein) accessible to the quencher (BCP), was close to unity, indicating thereby that both tryptophan residues of BSA are involved in dye-protein interaction. The rate constant for quenching, greater than 1010M-1s-1, indicated that the dye binding site is in close proximity to tryptophan residue of BSA. Thermodynamic parameters, obtained from data at different temperatures, showed that the binding of BCP to BSAinvolves hydrophobic bonds predominantly. Fluorescence intensity data in the presence of additives showed that hydrophobic interaction plays a prominent role. Significant decrease in concentration of free dye was observed for BCP in presence of paracetamol. Circular dichroism studies revealed the change in helicity of BSA, due to binding of BCP to BSA.
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