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Wyszukujesz frazę "polysialic acid" wg kryterium: Temat


Wyświetlanie 1-2 z 2
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:
Purification and characterization of GlcNAc-6-P 2-epimerase from Escherichia coli K92
Autorzy:
Ferrero, Miguel
Martínez-Blanco, Honorina
Lopez-Velasco, Federico
Ezquerro-Sáenz, Carlos
Navasa, Nicolas
Lozano, Sofia
Rodríguez-Aparicio, Leandro
Powiązania:
https://bibliotekanauki.pl/articles/1041092.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
sialic acid
capsular polysialic acid
N-acetylglucosamine
2-epimerase
Opis:
N-Acetylmannosamine (ManNAc) is the first committed intermediate in sialic acid metabolism. Thus, the mechanisms that control intracellular ManNAc levels are important regulators of sialic acid production. In prokaryotic organisms, UDP-N-acetylglucosamine (GlcNAc) 2-epimerase and GlcNAc-6-P 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc-6-P, respectively. We have purified for the first time native GlcNAc-6-P 2-epimerase from bacterial source to apparent homogeneity (1 200 fold) using Butyl-agarose, DEAE-FPLC and Mannose-6-P-agarose chromatography. By SDS/PAGE the pure enzyme showed a molecular mass of 38.4 ± 0.2 kDa. The maximum activity was achieved at pH 7.8 and 37°C. Under these conditions, the Km calculated for GlcNAc-6-P was 1.5 mM. The 2-epimerase activity was activated by Na+ and inhibited by mannose-6-P but not mannose-1-P. Genetic analysis revealed high homology with bacterial isomerases. GlcNAc-6-P 2-epimerase from E. coli K92 is a ManNAc-inducible protein and is detected from the early logarithmic phase of growth. Our results indicate that, unlike UDP-GlcNAc 2-epimerase, which promotes the biosynthesis of sialic acid, GlcNAc-6-P 2-epimerase plays a catabolic role. When E. coli grows using ManNAc as a carbon source, this enzyme converts the intracellular ManNAc-6-P generated into GlcNAc-6-P, diverting the metabolic flux of ManNAc to GlcNAc.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 387-399
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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