About: Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • Magnetic hydrogel microsheres were prepared by dispersion copolymerisation of 2-hydroxyethyl methacrylate and ethylene dimethacrylate in the presence of magnetite, which formed the core of the particles. RNase A was coupled to the particles by the cyanuric chloride method. Gel electrophoresis of plasmid DNA pUC19 (contaminated by bacterial RNA) confirmed RNA degradation with the immobilized enzyme. The effect of temperature and pH on the relative activity of immobilized RNase A was estimated after incubation of the samples at different temperatures (30-80 C) and pH (4.0-8.0). Maximum relative activity was observed at 70 C and pH 6.5. The matrice based on magnetic poly(HEMA) had a low tendency to adsorb RNA.
  • Magnetic hydrogel microsheres were prepared by dispersion copolymerisation of 2-hydroxyethyl methacrylate and ethylene dimethacrylate in the presence of magnetite, which formed the core of the particles. RNase A was coupled to the particles by the cyanuric chloride method. Gel electrophoresis of plasmid DNA pUC19 (contaminated by bacterial RNA) confirmed RNA degradation with the immobilized enzyme. The effect of temperature and pH on the relative activity of immobilized RNase A was estimated after incubation of the samples at different temperatures (30-80 C) and pH (4.0-8.0). Maximum relative activity was observed at 70 C and pH 6.5. The matrice based on magnetic poly(HEMA) had a low tendency to adsorb RNA. (en)
  • Magnetic hydrogel microsheres were prepared by dispersion copolymerisation of 2-hydroxyethyl methacrylate and ethylene dimethacrylate in the presence of magnetite, which formed the core of the particles. RNase A was coupled to the particles by the cyanuric chloride method. Gel electrophoresis of plasmid DNA pUC19 (contaminated by bacterial RNA) confirmed RNA degradation with the immobilized enzyme. The effect of temperature and pH on the relative activity of immobilized RNase A was estimated after incubation of the samples at different temperatures (30-80 C) and pH (4.0-8.0). Maximum relative activity was observed at 70 C and pH 6.5. The matrice based on magnetic poly(HEMA) had a low tendency to adsorb RNA. (cs)
Title
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres (en)
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres (cs)
skos:prefLabel
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres (en)
  • Properties of RNase A immobilized on magnetic poly(2-hydroxyethyl methacrylate) microspheres (cs)
skos:notation
  • RIV/00216224:14310/01:00004811!RIV08-GA0-14310___
http://linked.open.../vavai/riv/strany
  • 447
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/00/1339), P(KSK2050602), Z(AV0Z4050913)
http://linked.open...iv/cisloPeriodika
  • 3
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 693405
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/01:00004811
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Dispersion polymerization; RNase A; nucleic acids; particles; polystyrene; chromatography; purification (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [4EF8F6ACF075]
http://linked.open...i/riv/nazevZdroje
  • Biotechnology Progress
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 17
http://linked.open...iv/tvurceVysledku
  • Horák, Daniel
  • Rittich, Bohuslav
  • Šafář, Jan
  • Španová, Alena
  • Beneš, Milan J.
  • Lenfeld, Jiří
http://linked.open...n/vavai/riv/zamer
issn
  • 8756-7938
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 107 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software