Sample displacement chromatography (SDC) in reversed-phase and ion-exchange modes was introduced approximately twenty years ago. This method takes advantage of relative binding affinities of components in a sample mixture. During loading, there is a competition among different sample components for the sorption on the surface of the stationary phase. SDC was first used for the preparative purification of proteins. Later, it was demonstrated that this kind of chromatography can also be performed in ion-exchange, affinity and hydrophobic-interaction mode. It has also been shown that SDC can be performed on monoliths and membrane-based supports in both analytical and preparative scale. Recently, SDC in ion-exchange and hydrophobic interaction mode was also employed successfully for the removal of trace proteins from monoclonal antibody preparations and for the enrichment of low abundance proteins from human plasma. In this review, the principals of SDC are introduced, and the potential for separation of proteins and peptides in micro-analytical, analytical and preparative scale is discussed.
Preparative purification of peptides by reversed-phase chromatography. Sample displacement mode versus gradient elution mode
Development of simultaneous purification methodology for multiple synthetic peptides by reversed-phase sample displacement chromatography
Selective enrichment of low-abundance peptides in complex mixtures by elution-modified displacement chromatography and their identification by electrospray ionization mass spectrometry
Preparative reversed-phase liquid chromatography of proteins from rabbit skeletal troponin, a multi-protein complex
Preparation of vitamin K-dependent proteins, such as clotting factors II, VII, IX and X and clotting inhibitor protein C
Anion-exchange chromatography using short monolithic columns as a complementary technique for human serum albumin depletion prior to human plasma proteome analysis
Use of multidimensional separation protocols for the purification of trace components in complex biological samples for proteomics analysis
Evaluation of three principally different intact protein prefractionation methods for plasma biomarker discovery
Occurrence of autoantibodies to annexin I, 14-3-3 theta and LAMR1 in prediagnostic lung cancer sera.
Peptide mapping with mobile phases of intermediate pH value using capillary reversed-phase high-performance liquid chromatography/electrospray ionisation tandem mass spectrometry
Application of displacement chromatography for the proteome analysis of a human plasma protein fraction
Solubility and binding properties of PEGylated lysozyme derivatives with increasing molecular weight on hydrophobic-interaction chromatographic resins
Unique selectivity windows using selective displacers/eluents and mobile phase modifiers on hydroxyapatite
Selectivity of monolithic supports under overloading conditions and their use for separation of human plasma and isolation of low abundance proteins
Therapeutic plasma proteins--application of proteomics in process optimization, validation, and analysis of the final product
A pipeline that integrates the discovery and verification of plasma protein biomarkers reveals candidate markers for cardiovascular disease.
Anion-exchange purification of recombinant factor IX from cell culture supernatant using different chromatography supports
Comparison of displacement versus gradient mode for separation of a complex protein mixture by anion-exchange chromatography
Expression, stabilization and purification of membrane proteins via diverse protein synthesis systems and detergents involving cell-free associated with self-assembly peptide surfactants
Multiple, simultaneous, independent gradients for a versatile multidimensional liquid chromatography. Part II: Application 1 - Large increases in isoform resolution of human transferrin by use of dual simultaneous independent gradients of pH & acetonitrile on a mixed bed (anion exchange plus reversed phase) stationary phase
Polymethacrylate-based monoliths as stationary phases for separation of biopolymers and immobilization of enzymes
Blood Clotting Disorders
Thrombophilia includes conditions with increased tendency for excessive blood clotting. Blood clotting occurs when the body has insufficient amounts of specialized proteins that make blood clot and stop bleeding. Here is the latest research on blood clotting disorders.