Identification and relative quantification of membrane proteins by surface biotinylation and two-dimensional peptide mapping

• Published in: Proteomics (Weinheim) Vol. 5; no. 11; pp. 2718 - 2728
• Main Authors: Scheurer, Simone B., Rybak, Jascha-N., Roesli, Christoph, Brunisholz, René A., Potthast, Frank, Schlapbach, Ralph, Neri, Dario, Elia, Giuliano
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01.07.2005; WILEY‐VCH Verlag; Wiley-VCH
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Biotinylation - methods; Blotting, Western; Cells, Cultured; Chromatography, High Pressure Liquid; Electrophoresis, Gel, Two-Dimensional; Endothelial Cells - chemistry; Endothelium, Vascular - chemistry; Endothelium, Vascular - cytology; Fundamental and applied biological sciences. Psychology; Human umbilical vein endothelial cells; Humans; Hypoxia; Kidney - chemistry; Kidney - embryology; Mass spectrometry; Membrane proteins; Membrane Proteins - isolation & purification; Membrane Proteins - metabolism; Miscellaneous; Peptide analysis; Peptide Mapping - methods; Proteins; Serum Albumin, Bovine; Software; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Surface biotinylation; Umbilical Veins - cytology; Human; Endothelial cell; Oxygen; Membrane protein; Human umbilical vein endothelial cells; Biotinylation; Peptides; Identification; Membrane proteins; Surface biotinylation; Proteomics; Hypoxia; Peptide analysis; Mass spectrometry; Quantitative analysis

Membrane proteins play a central role in biological processes, but their separation and quantification using two‐dimensional gel electrophoresis is often limited by their poor solubility and relatively low abundance. We now present a method for the simultaneous recovery, separation, identification,...