About: Retention behavior of a homologous series and positional isomers of aliphatic amino acids in hydrophilic interaction chromatography     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
rdfs:seeAlso
Description
  • The retention behavior of several series of free alpha- and omega-amino acids and positional isomers of amino pentanoic acid in the hydrophilic interaction chromatography mode (HILIC) was studied. The study was carried out on three stationary phases followed by post-column derivatization with fluorescence detection in order to describe the retention mechanism of the tested amino acids. The effect of chromatographic conditions including acetonitrile content in the mobile phase, mobile phase pH (ranging from 3.5 to 6.5) and concentration of buffer in the mobile phase was investigated. The effect of the number of carbon atoms (n(C)) in aliphatic chains of the individual homologue of alpha- and omega-amino acids and the logarithm of the partition coefficient (logD) on retention was also a part of the presented study. A good correlation (r > 0.98) between the logk and logD values of amino acids or n(C), respectively, was observed. The described linear relationships were subsequently applied to predict the retention behavior of individual members of the homologous series of amino acids and to optimize the mobile phase composition in HILIC. The obtained results confirmed that the retention mechanism of alpha-amino acids, omega-amino acids and positional isomers of amino acids was based on the logD values and the number of carbon atoms in the aliphatic chains of amino acids. The elution order of omega-amino acids and positional isomers of amino pentanoic acid was strongly dependent on the mobile phase pH in the investigated range whereas the retention factors of all alpha-amino acids remained essentially unchanged on all tested stationary phases.
  • The retention behavior of several series of free alpha- and omega-amino acids and positional isomers of amino pentanoic acid in the hydrophilic interaction chromatography mode (HILIC) was studied. The study was carried out on three stationary phases followed by post-column derivatization with fluorescence detection in order to describe the retention mechanism of the tested amino acids. The effect of chromatographic conditions including acetonitrile content in the mobile phase, mobile phase pH (ranging from 3.5 to 6.5) and concentration of buffer in the mobile phase was investigated. The effect of the number of carbon atoms (n(C)) in aliphatic chains of the individual homologue of alpha- and omega-amino acids and the logarithm of the partition coefficient (logD) on retention was also a part of the presented study. A good correlation (r > 0.98) between the logk and logD values of amino acids or n(C), respectively, was observed. The described linear relationships were subsequently applied to predict the retention behavior of individual members of the homologous series of amino acids and to optimize the mobile phase composition in HILIC. The obtained results confirmed that the retention mechanism of alpha-amino acids, omega-amino acids and positional isomers of amino acids was based on the logD values and the number of carbon atoms in the aliphatic chains of amino acids. The elution order of omega-amino acids and positional isomers of amino pentanoic acid was strongly dependent on the mobile phase pH in the investigated range whereas the retention factors of all alpha-amino acids remained essentially unchanged on all tested stationary phases. (en)
Title
  • Retention behavior of a homologous series and positional isomers of aliphatic amino acids in hydrophilic interaction chromatography
  • Retention behavior of a homologous series and positional isomers of aliphatic amino acids in hydrophilic interaction chromatography (en)
skos:prefLabel
  • Retention behavior of a homologous series and positional isomers of aliphatic amino acids in hydrophilic interaction chromatography
  • Retention behavior of a homologous series and positional isomers of aliphatic amino acids in hydrophilic interaction chromatography (en)
skos:notation
  • RIV/00216208:11160/14:10282195!RIV15-MSM-11160___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, S
http://linked.open...iv/cisloPeriodika
  • 7
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
  • 42541
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11160/14:10282195
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Retention behavior; Homologous series; HILIC; Amino acids (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV
  • [125CEA04A388]
http://linked.open...i/riv/nazevZdroje
  • Journal of Separation Science
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 37
http://linked.open...iv/tvurceVysledku
  • Nováková, Lucie
  • Douša, Michal
  • Gibala, Petr
  • Stránský, Zdeněk
  • Srbek, Jan
http://linked.open...ain/vavai/riv/wos
  • 000333538600001
issn
  • 1615-9306
number of pages
http://bibframe.org/vocab/doi
  • 10.1002/jssc.201301348
http://localhost/t...ganizacniJednotka
  • 11160
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, 75 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software