McDonald, Claudia A. published the artcileCombining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome, Computed Properties of 85618-21-9, the publication is Molecular and Cellular Proteomics (2009), 8(2), 287-301, database is CAplus and MEDLINE.
Identification of glycosylated proteins, especially those in the plasma membrane, has the potential of defining diagnostic biomarkers and therapeutic targets as well as increasing the understanding of changes occurring in the glycoproteome during normal differentiation and disease processes. Although many cellular proteins are glycosylated they are rarely identified by mass spectrometric anal. (e.g. shotgun proteomics) of total cell lysates. Therefore, methods that specifically target glycoproteins are necessary to facilitate their isolation from total cell lysates prior to their identification by mass spectrometry-based anal. To enrich for plasma membrane glycoproteins the methods must selectively target characteristics associated with proteins within this compartment. The authors demonstrate that the application of two methods, one that uses periodate to label glycoproteins of intact cells and a hydrazide resin to capture the labeled glycoproteins and another that targets glycoproteins with sialic acid residues using lectin affinity chromatog., in conjunction with liquid chromatog.-tandem mass spectrometry is effective for plasma membrane glycoprotein identification. The authors demonstrate that this combination of methods dramatically increases coverage of the plasma membrane proteome (more than one-half of the membrane glycoproteins were identified by the two methods uniquely) and also results in the identification of a large number of secreted glycoproteins. The authors’ approach avoids the need for subcellular fractionation and utilizes a simple detergent lysis step that effectively solubilizes membrane glycoproteins. The plasma membrane localization of a subset of proteins identified was validated, and the dynamics of their expression in HeLa cells was evaluated during the cell cycle. Results obtained from the cell cycle studies demonstrate that plasma membrane protein expression can change up to 4-fold as cells transit the cell cycle and demonstrate the need to consider such changes when carrying out quant. proteomics comparison of cell lines.
Molecular and Cellular Proteomics published new progress about 85618-21-9. 85618-21-9 belongs to alcohols-buliding-blocks, auxiliary class Tetrahydropyran,Chiral,sulfides,Alcohol, name is (2R,3S,4S,5R,6S)-2-(Hydroxymethyl)-6-(octylthio)tetrahydro-2H-pyran-3,4,5-triol, and the molecular formula is C14H28O5S, Computed Properties of 85618-21-9.
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