Oligomeric structure of bAE3 protein

A. V. Pushkin, V. L. Tsuprun, N. K. Abuladze, D. Newman

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


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 x 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.

Original languageEnglish (US)
Pages (from-to)397-401
Number of pages5
JournalIUBMB Life
Issue number6
StatePublished - Jan 1 2000


  • AE3
  • Electron microscopy
  • Oligomeric structure
  • Rabbit kidney


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