Analysis of Molecular Masses and Oligomeric States of Protein Complexes by Blue Native Electrophoresis and Isolation of Membrane Protein Complexes by Two-Dimensional Native Electrophoresis
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Abstract
Blue native Electrophoresis is a "charge shift" method developed for isolation of
native membrane protein complexes from biological membranes that also separates both
acidic and basic water-soluble proteins at a fixed pH of 7.5. In combination with
a second dimension sodium dodecylsulfate electrophoresis it provides an analytical
method for the determination of molecular mass and oligomeric state of nondissociated
complexes, of subunit composition, and of degree of purity and for the detection of
subcomplexes. The method was applied to analysis of cytochrome bc/bf complexes. By
combination of a novel colorless native polyacrylamide gel electrophoresis (CN-PAGE)
with blue native BN-PAGE, a two-dimensional native technique was developed that is
suitable for preparation of highly pure membrane protein complexes.