Reference : Comparison of three methods for fractionation and enrichment of low molecular weight ...
Scientific journals : Article
Human health sciences : Pharmacy, pharmacology & toxicology
http://hdl.handle.net/2268/8787
Comparison of three methods for fractionation and enrichment of low molecular weight proteins for SELDI-TOF-MS differential analysis
English
De Bock, Muriel mailto [Université de Liège - ULg > > > GIGA - Membres]
De Seny, Dominique mailto [Université de Liège - ULg > > Rhumatologie >]
Meuwis, Marie-Alice mailto [Université de Liège - ULg > > GIGA-Management : Plate-forme protéomique >]
Servais, Anne-Catherine mailto [Université de Liège - ULg > Département de pharmacie > Analyse des médicaments >]
Minh, Tran Quang [Affiland > > > >]
Closset, Jean mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Département des sciences biomédicales et précliniques >]
Chapelle, Jean-Paul mailto [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Louis, Edouard mailto [Université de Liège - ULg > Département des sciences cliniques > Hépato-gastroentérologie - Relations académiques et scientifiques (Médecine) >]
Malaise, Michel mailto [Université de Liège - ULg > Département des sciences cliniques > Rhumatologie >]
Merville, Marie-Paule mailto [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Fillet, Marianne mailto [Université de Liège - ULg > Département de pharmacie > Analyse des médicaments >]
2010
Talanta
Elsevier Science
82
245-254
Yes (verified by ORBi)
International
0039-9140
1873-3573
Amsterdam
The Netherlands
[en] Protein prefractionation ; Major protein depletion ; Plasma ; Serum ; SELDI-TOF-MS
[en] In most diseases, the clinical need for serum/plasma markers has never been so crucial, not only for diagnosis, but also for the selection of the most efficient therapies, as well as exclusion of ineffective or toxic treatment. Due to the high sample complexity, prefractionation is essential for exploring the deep proteome and finding specific markers.
In this study, three different sample preparation methods (i.e., highly abundant protein precipitation, restricted access materials (RAM) combined with IMAC chromatography and peptide ligand affinity beads) were investigated in order to select the best fractionation step for further differential proteomic experiments focusing on the LMW proteome (MW inferior to 40,000 Da). Indeed, the aim was not to cover the entire plasma/serum proteome, but to enrich potentially interesting tissue leakage proteins. These three methods were evaluated on their reproducibility, on the SELDI-TOF-MS peptide/protein peaks generated after fractionation and on the information supplied.
The studied methods appeared to give complementary information and presented good reproducibility (below 20%). Peptide ligand affinity beads were found to provide efficient depletion of HMW proteins and peak enrichment in protein/peptide profiles.
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds Léon Fredericq ; Centre Anti-Cancéreux ; Télévie
http://hdl.handle.net/2268/8787

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