Journal
IUBMB LIFE
Volume 50, Issue 6, Pages 397-401Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/152165400300089493
Keywords
AE3; electron microscopy; oligomeric structure; rabbit kidney
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Funding
- NIDDK NIH HHS [DK58563, DK46976, DK07789] Funding Source: Medline
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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 similar to 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 (similar to 11-14 nm) and square-shaped (similar to 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.
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