title: Solid-phase fractionation strategies applied to proteomics investigations.
abstract: Methods for protein fractionation in the proteomics investigation field are relatively numerous. They apply to the prefractionation of the sample to obtain less complex protein mixtures for an easier analysis; they are also used as a means to evidence specific proteins or protein classes otherwise impossible to detect. They involve depletion of high-abundance proteins suppressing the signal of dilute species; they are also capable to enhance the detectability of low-abundance species while concomitantly decreasing the concentration of abundant proteins such as albumin in serum and hemoglobin in red blood cell lysates. Fractionation of proteomes is also used for the isolation of targeted species that are selected for their different expression under certain pathological conditions and that are detected by mass spectrometry. Two unconventional methods of large interest in proteomics due to the low level of protein redundancy between fractions are also reported.All these methods are reviewed and detailed method given to allow specialists of proteomics investigation to access selected separation methods generally dispersed on different technical reviews or books.
authors.affiliation: Bio-Rad Laboratories, Marnes la Coquette, France.
authors.forename: Luc
authors.initials: L
authors.lastname: Guerrier
authors.forename: Frederic
authors.initials: F
authors.lastname: Fortis
authors.forename: Egisto
authors.initials: E
authors.lastname: Boschetti
mesh_terms: D053000:Analytic Sample Preparation Methods; D002021:Buffers; D002845:Chromatography; D006023:Glycoproteins / Q000032:analysis / Q000302:isolation & purification; D006801:Humans; D008863:Microspheres; D010750:Phosphoproteins / Q000032:analysis / Q000302:isolation & purification; D040901:Proteomics / Q000379:methods*; D052616:Solid Phase Extraction / Q000379:methods*
chemical_list: D002021:Buffers; D006023:Glycoproteins; D010750:Phosphoproteins