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- Title
Oligomeric Structure of bAE3 Protein.
- Authors
Pushkin, Alexander V.; Tsuprun, Vladimir L.; Abuladze, Natalia K.; Newman, Debra; Kurtz, Ira
- Abstract
The "brain" form of the anion exchanger protein 3 (bAE3) has been purified to homogeneity from the rabbit kidney by differential centrifugation and immunoaffinity chromatography. A single protein band of ∼ 165 kDa was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Monomers, dimers (a major component), and a higher oligomeric form (apparently tetramers) were found after oxidative cross-linking of purified bAE3. The largest form of bAE3 was separated from dimers and monomers by sucrose gradient centrifugation and was studied by transmission electron microscopy to confirm a tetrameric structure. Two main types of bAE3 images were detected, round (∼11-14 nm) and square-shaped (∼12×12 nm). Image analysis revealed fourfold rotational symmetry of both the round and square-shaped images, indicating that bAE3 consists of multiples of 4 subunits. We conclude that bAE3 in Triton X-100 solution is predominantly a mixture of dimers and tetramers with a smaller amount of monomers.
- Subjects
ANIONS; PROTEINS; MONOMERS; DIMERS
- Publication
IUBMB Life, 2000, Vol 50, Issue 6, p397
- ISSN
1521-6543
- Publication type
Article
- DOI
10.1080/152165400300089493