title: Native polyacrylamide gels.
abstract: Usually proteins are separated by polyacrylamide gel electrophoresis (PAGE) in the presence of a detergent and under (heat-) denaturing and (non- or) reducing conditions. The most commonly used detergent is sodium dodecyl sulfate (SDS). The major function of SDS is to shield the respective charge of the proteins present in the mixture to be analyzed and to provide all proteins with a negative charge. As a consequence, the proteins will be separated according to their molecular weight. Electrophoresis of proteins can also be performed in the absence of SDS. Using such "native" conditions, the charge of each of the proteins, which will depend on the primary amino acid sequence of the protein (isoelectric point) and the pH during electrophoresis, will mainly influence the mobility of the respective protein during electrophoresis. Here we describe a starting protocol for "native" PAGE.
authors.affiliation: Carl Gustav Carus University TU Dresden, Dresden, Germany.
authors.forename: Claudia
authors.initials: C
authors.lastname: Arndt
authors.forename: Stefanie
authors.initials: S
authors.lastname: Koristka
authors.forename: Holger
authors.initials: H
authors.lastname: Bartsch
authors.forename: Michael
authors.initials: M
authors.lastname: Bachmann
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002021:Buffers; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D002021:Buffers; D011506:Proteins; D012710:Serum Albumin, Bovine