title: Novel hydrophobic standards for membrane protein molecular weight determinations via sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
abstract: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally employed technique that separates proteins on the basis of molecular weight (MW). However, membrane proteins are known to size anomalously on SDS-PAGE calibrated with conventional standards, an issue that complicates interpretation of protein identity, purity, degradation, and/or stoichiometry. Here we describe the preparation of novel polyleucine hydrophobic standards for SDS-PAGE that reduce the average deviation of the apparent MW from the formula MW of natural membrane proteins to 7% versus 20% with commercially available standards. Our results suggest that gel calibration with hydrophobic standards may facilitate the interpretation of membrane protein SDS-PAGE experiments.
authors.affiliation: Division of Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Toronto, Ontario, Canada M5G 1X8.
authors.forename: Arianna
authors.initials: A
authors.lastname: Rath
authors.forename: Vincent G
authors.initials: VG
authors.lastname: Nadeau
authors.forename: Bradley E
authors.initials: BE
authors.lastname: Poulsen
authors.forename: Derek P
authors.initials: DP
authors.lastname: Ng
authors.forename: Charles M
authors.initials: CM
authors.lastname: Deber
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008970:Molecular Weight
chemical_list: D008565:Membrane Proteins