Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "horseradish" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-5 z 5
    Tytuł:
    Controllable preparation of highly active horseradish peroxidase-gold nanoparticle bionanoconjugate
    Autorzy:
    Zhang, P.
    Liu, Ch.
    Song, S.
    Peng, Ch.
    Powiązania:
    https://bibliotekanauki.pl/articles/778931.pdf
    Data publikacji:
    2012
    Wydawca:
    Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
    Tematy:
    horseradish peroxidase
    gold nanoparticles
    bionanoconjugate
    Opis:
    A novel method of immobilizing horse radish peroxidase enzyme (HRP) onto the surface of gold nanoparticles (GNPs) was developed. As a result, a high-activity bionanoconjugates was obtained through utilizing the biotin-streptavidin (SA) system. The HRP-SA-GNP bionanoconjugate with high activity was conveniently prepared through the biotin- avidin system. Compared with the HRP-GNP bioconjugate prepared through the traditional electrostatic absorption method, the enzyme activity per GNPs of this new bionanoconjugate was enhanced by 10 times. Moreover, the enzyme activity of this bionanoconjugate was controllable. The above method of bionanoconjugation preparation has promising applications In the fi elds including preparing highly active bio-nanoprobe and immobilized enzyme.
    Źródło:
    Polish Journal of Chemical Technology; 2012, 14, 4; 57-60
    1509-8117
    1899-4741
    Pojawia się w:
    Polish Journal of Chemical Technology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Enzymatic assay of opioid analgesic, tramadol, using horseradish peroxidase
    Autorzy:
    Sridevi, N.
    Srilakshmi, C.
    Alekya, G.
    Bala Sekaran, C.
    Powiązania:
    https://bibliotekanauki.pl/articles/10767.pdf
    Data publikacji:
    2014
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    opioid
    tramadol
    horseradish peroxidase
    enzymatic method
    Opis:
    Three novel and sensitive enzymatic methods have been developed for the quantification of tramadol in pharmaceutical dosage forms. The proposed methods are based on the reaction of tramadol with 3-methylbenzothiazoline-2-one hydrazone (method A), aniline (method B) and aminoantipyrine in the presence of hydrogen peroxide and horseradish peroxidase to give colored complexes. The colored complexes obtained with 3-methylbenzothiazoline-2-one hydrazone, aniline and aminoantipyrine exhibit absorption maxima at 480 nm, 550 nm and 530 nm, respectively. Regression analysis of Beer’s plots showed good correlation for tramadol in the concentration range (μg/mL) 2-12 for the methods A & B and 4-24 for the method C. The experimental parameters were studied and optimized. The precision and accuracy of the methods were satisfactory. The proposed methods were successfully applied for the quantification of tramadol in 3 brands of commercially available tablet dosage forms. The results were compared satisfactorily with the official method.
    Źródło:
    International Letters of Natural Sciences; 2014, 11, 1
    2300-9675
    Pojawia się w:
    International Letters of Natural Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase
    Autorzy:
    Gębicka, Lidia
    Powiązania:
    https://bibliotekanauki.pl/articles/1044450.pdf
    Data publikacji:
    1999
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    lactoperoxidase
    nitrite
    stopped-flow
    horseradish peroxidase
    Opis:
    The reaction of nitrite (NO-_2) with horseradish peroxidase and lactoperoxidase was studied. Sequential mixing sopped-flow measeruments gave the following values for the rate constants of the reaction of nitrite with compounds II (oxoferryl heme intermediates) of horseradish peroxidase and lactoperoxidase at pH 7.0, 13.3 ± 0.07 mol^{-1}dm^3s^{-1} and 3.5 ± 0.05 · 10^4mol^{-1}dm^3s^{-1}, respectively. Nitrite, at neutral pH, influenced measurements of activity of lactoperoxidase with typical substrates like 2,2'-azino-bis[ethyl-benzothiazoline-(6)-sulphonic acid] (ABTS), guaiacol or thiocyanate (SCN-). The rate of ABTS and guaiacol oxidation increased linearly with nitrite concentration up to 2.5-5 mmol dm^{-3}. On the other hand, two-electron SCN- oxidation was inhibited in the presence od nitrite. Thus, nitrite competed with the investigated substrates of lactoperoxidase. The intermediate, most probably nitrogen dioxide (*NO_2), reacted more rapidly with ABTS or guaiacol than did lactoperoxidase compound II. It did not, however, effectively oxidize SCN- to OSCN-. NO-_2 did not influence the activity measurements of horseradish peroxidase by ABTS or guaiacol method.
    Źródło:
    Acta Biochimica Polonica; 1999, 46, 4; 919-927
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Application of TSA technique in localization of snRNP-rich cytoplasmic bodies
    Autorzy:
    Hyjek, M.
    Wojciechowska, N.
    Kolowerzo, A.
    Smolinski, D.J.
    Powiązania:
    https://bibliotekanauki.pl/articles/80402.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    RNA maturation
    eukaryotic cell
    biogenesis
    TSA technique
    microsporocyte
    catalytic activity
    horseradish peroxidase
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Enzymatic oxidation of neobetanin monitored by liquid chromatography with mass spectrometric detection
    Autorzy:
    Starzak, K.
    Szot, D.
    Skopińska, A.
    Swiergosz, T.
    Wybraniec, S.
    Powiązania:
    https://bibliotekanauki.pl/articles/115945.pdf
    Data publikacji:
    2016
    Wydawca:
    Fundacja na Rzecz Młodych Naukowców
    Tematy:
    neobetanin
    betalains
    betacyanins
    horseradish peroxidase
    oxidation
    enzymatic
    spectrophotometry
    mass spectrometry
    chromatography
    neobetanina
    betalainy
    betacyjaniny
    peroksydaza chrzanowa
    enzymatyczne utlenianie
    spektrofotometria
    spektrometria masowa
    chromatografia
    Opis:
    The aim of this study was monitoring of enzymatic oxidation of neobetanin, an interesting type of betalains which is a partially oxidized betacyanin. As it belongs to betalains, it is water soluble and non-toxic, but a presence of a few functional groups makes it very reactive. Oxidation reactions were performed using horseradish peroxidase followed by spectrophotometric and mass spectrometric detection (LC-DAD-ESI-MS/MS) of obtained products. Enzymatic oxidation of neobetanin leads to a formation of new decarboxy- and dehydro-derivatives. The main identified oxidation product is 2-decarboxy-2,3-dehydroneobetanin. Searching for all formed oxidation products is extremely important for elucidation of the betalains oxidation mechanism.
    Źródło:
    Challenges of Modern Technology; 2016, 7, 1; 29-31
    2082-2863
    2353-4419
    Pojawia się w:
    Challenges of Modern Technology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies