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  • Lactoferrin is considered a multifunctional or multi-tasking protein. It appears to play several biological roles, whereas its structure is very crucial. The aim of this work was to investigate basic electrochemical behaviour of lactoferrin by both stationary and flow electrochemical methods with respect to study of structural changes of the compound of interest. The behaviour of lactoferrin was studied by three various electrochemical methods (linear sweep, differential pulse and square wave voltammetry). Based on the results obtained, we utilized flow injection analysis with electrochemical detection for determination of lactoferrin. We found out that the most suitable FIA-ED conditions were as follows: working electrode potential of 900 mV, Britton-Robinson buffer (pH 4.5) as mobile phase, its flow rate 1 ml.min-1. The detection limit was about tens of ng per ml. Finally, we attempted to follow the changes of lactoferrin signal in the presence of chemical compounds or under the physical conditions
  • Lactoferrin is considered a multifunctional or multi-tasking protein. It appears to play several biological roles, whereas its structure is very crucial. The aim of this work was to investigate basic electrochemical behaviour of lactoferrin by both stationary and flow electrochemical methods with respect to study of structural changes of the compound of interest. The behaviour of lactoferrin was studied by three various electrochemical methods (linear sweep, differential pulse and square wave voltammetry). Based on the results obtained, we utilized flow injection analysis with electrochemical detection for determination of lactoferrin. We found out that the most suitable FIA-ED conditions were as follows: working electrode potential of 900 mV, Britton-Robinson buffer (pH 4.5) as mobile phase, its flow rate 1 ml.min-1. The detection limit was about tens of ng per ml. Finally, we attempted to follow the changes of lactoferrin signal in the presence of chemical compounds or under the physical conditions (en)
  • Nový nástroj pro rozdělení rozdílných strukturních forem laktoferinu (cs)
Title
  • A new tool for distinguishing of different structural forms of lactoferrin
  • A new tool for distinguishing of different structural forms of lactoferrin (en)
  • Nový nástroj pro rozdělení rozdílných strukturních forem laktoferinu (cs)
skos:prefLabel
  • A new tool for distinguishing of different structural forms of lactoferrin
  • A new tool for distinguishing of different structural forms of lactoferrin (en)
  • Nový nástroj pro rozdělení rozdílných strukturních forem laktoferinu (cs)
skos:notation
  • RIV/00216224:14310/07:00022110!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • A635-A635
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM0021622412)
http://linked.open...iv/cisloPeriodika
  • 5
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
  • 408028
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/07:00022110
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • distinguish; structural forms; lactoferrin; FIA-ED (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [FAA0D9F6029A]
http://linked.open...i/riv/nazevZdroje
  • Faseb J.
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 21
http://linked.open...iv/tvurceVysledku
  • Adam, Vojtěch
  • Kizek, René
  • Stejskal, Karel
  • Trnková, Libuše
  • Zehnálek, Josef
  • Zítka, Ondřej
  • Havel, L.
  • Zeman, L.
  • Kukačka, J.
  • Průša, R.
  • Horna, A.
http://linked.open...n/vavai/riv/zamer
issn
  • 0892-6638
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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