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
—