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Characterization of deoxyribonuclease I immobilized on magnetic hydrophilic polymer particles

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00006659" target="_blank" >RIV/00216224:14310/02:00006659 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Characterization of deoxyribonuclease I immobilized on magnetic hydrophilic polymer particles

  • Original language description

    Magnetic bead cellulose particles and magnetic poly(HEMA-co-EDMA) microsheres with immobilized DNaseI were used for degradation of chromosomal and plasmid DNAs. Divalent cations (Mg2+,Ca2+,Mn2+ and Co2+) were used for the activation of DNaseI. A comparison of free and immobilized enzyme (magnetic bead particles) activities was carried out in dependence on pH and activating cation. The maximum of the activity of immobilized DNaseI was shifted to lower pH compared with free DNaseI. DNaseI immobilized ön magnetic bead cellulose was used 20 times in the degradation of chromosomal DNA. Its residual activity was influenced by the nature of activating divalent cation. The immobilized enzyme with decreased activity was reactivated by Co2+ ions.

  • Czech name

    Characterization of deoxyribonuclease I immobilized on magnetic hydrophilic polymer particles

  • Czech description

    Magnetic bead cellulose particles and magnetic poly(HEMA-co-EDMA) microsheres with immobilized DNaseI were used for degradation of chromosomal and plasmid DNAs. Divalent cations (Mg2+, Ca2+, Mn2+ and Co2+) were used for the activation of DNaseI. A comparison of free and immobilized enzyme (magnetic bead particles) activities was carried out in dependence on pH and activating cation. The maximum of the activity of immobilized DNaseI was shifted to lower pH compared with free DNase I. DNase I immobilizedon magnetic bead cellulose was used 20 times in the degradation of chromosomal DNA. Its residual activity was influenced by the nature of activating divalent cation. The immobilized enzyme with decreased activity was reactivated by Co2+ ions.

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EI - Biotechnology and bionics

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2002

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Chromatography B

  • ISSN

    1570-0232

  • e-ISSN

  • Volume of the periodical

    2002

  • Issue of the periodical within the volume

    774

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    25-31

  • UT code for WoS article

  • EID of the result in the Scopus database