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Wyszukujesz frazę "Kinetic analysis" wg kryterium: Wszystkie pola


Wyświetlanie 1-4 z 4
Tytuł:
Translocation of polysialic acid across model membranes: Kinetic analysis and dynamic.
Autorzy:
Janas, Teresa
Krajiński, Henryk
Timoszyk, Anna
Janas, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044181.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
polysialic acid
1H-NMR
electrical equivalent circuit
polycation flux
polyanion flux
lipid bilayers
membrane transport
Opis:
Transmembrane translocation of polyion homopolymers takes place in the case of polyanionic polysialic acid (polySia), polyanionic polynucleotides and polycationic polypeptides. The purpose of this work was to determine the role of membrane electrical parameters on the kinetics of polyion translocation, the influence of polysialic acid on ion adsorption on positively charged membrane surface and the dynamics of the phospholipid hydrocarbon chains and choline group by using 1H-NMR. The analysis of polyion translocation was performed by using the electrical equivalent circuit of the membrane for the initial membrane potential equal to zero. The changes in polysialic acid flux was up to 75% after 1 ms in comparison with the zero-time flux. Both a decrease of membrane conductance and an increase of polyion chain length resulted in the diminution of this effect. An increase of praseodymium ions adsorption to positively charged liposomes and an increase of the rate of segmental movement of the -CH2 and -CH3 groups, and the choline headgrup of lipid molecules, was observed in the presence of polySia. The results show that the direction of the vectorial polyion translocation depends both on the membrane electrical properties and the degree of polymerization of the polymer, and that polysialic acid can modulate the degree of ion adsorption and the dynamics of membrane lipids.
Źródło:
Acta Biochimica Polonica; 2001, 48, 1; 163-173
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades
Autorzy:
Varón, Ramón
Havsteen, Bent
Valero, Edelmira
Molina-Alarcón, Milagros
García-Cánovas, Francisco
García-Moreno, Manuela
Powiązania:
https://bibliotekanauki.pl/articles/1041315.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
steady state
fractional modification
transient phase
enzyme kinetics
multicyclic cascades
Opis:
This paper presents a kinetic analysis of the whole reaction course, i.e. of both the transient phase and the steady state, of open multicyclic enzyme cascade systems. Equations for fractional modifications are obtained which are valid for the whole reaction course. The steady state expressions for the fractional modifications were derived from the latter equations since they are not restricted to the condition of rapid equilibrium. Finally, the validity of our results is discussed and tested by numerical integration. Apart from the intrinsic value of knowing the kinetic behaviour of any of the species involved in any open multicyclic enzyme cascade, the kinetic analysis presented here can be the basis of future contributions concerning open multicyclic enzyme cascades which require the knowledge of their time course equations (e.g. evaluation of the time needed to reach the steady state, suggestion of kinetic data analysis, etc.), analogous to those already carried out for open bicyclic cascades.
Źródło:
Acta Biochimica Polonica; 2005, 52, 4; 765-780
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Activity and kinetic properties of phosphotransacetylase from intestinal sulfate-reducing bacteria
Autorzy:
Kushkevych, Ivan
Powiązania:
https://bibliotekanauki.pl/articles/1039142.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
sulfate-reducing bacteria
phosphotransacetylase
kinetic analysis
inflammatory bowel diseases
Opis:
Phosphotransacetylase activity and the kinetic properties of the enzyme from intestinal sulfate-reducing bacteria Desulfovibrio piger and Desulfomicrobium sp. has never been well-characterized and has not been studied yet. In this paper, the specific activity of phosphotransacetylase and the kinetic properties of the enzyme in cell-free extracts of both D. piger Vib-7 and Desulfomicrobium sp. Rod-9 intestinal bacterial strains were presented at the first time. The microbiological, biochemical, biophysical and statistical methods in this work were used. The optimal temperature and pH for enzyme reaction was determined. Analysis of the kinetic properties of the studied enzyme was carried out. Initial (instantaneous) reaction velocity (V0), maximum amount of the product of reaction (Pmax), the reaction time (half saturation period, τ) and maximum velocity of the phosphotransacetylase reaction (Vmax) were defined. Michaelis constants (Km) of the enzyme reaction (3.36 ± 0.35 mM for D. piger Vib-7, 5.97 ± 0.62 mM for Desulfomicrobium sp. Rod-9) were calculated. The studies of the phosphotransacetylase in the process of dissimilatory sulfate reduction and kinetic properties of this enzyme in intestinal sulfate-reducing bacteria, their production of acetate in detail can be perspective for clarification of their etiological role in the development of the humans and animals bowel diseases. These studies might help in predicting the development of diseases of the gastrointestinal tract, by providing further details on the etiology of bowel diseases which are very important for the clinical diagnosis of these disease types.
Źródło:
Acta Biochimica Polonica; 2015, 62, 1; 103-108
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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