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Brain Res Mol Brain Res. 1993 Apr;18(1-2):87-99.

The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences.

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Department of Structural and Cellular Biology, University of South Alabama, School of Medicine, Mobile 36688.

Erratum in

  • Brain Res Mol Brain Res 1993 Oct;20(1-2):179.
  • Brain Res Mol Brain Res 1994 Jan;21(1-2):181.
  • Brain Res Mol Brain Res 1995 May;30(1):176.


The amino acid sequence of mouse brain beta spectrin (beta fodrin), deduced from the nucleotide sequence of complementary DNA clones, reveals that this non-erythroid beta spectrin comprises 2363 residues, with a molecular weight of 274,449 Da. Brain beta spectrin contains three structural domains and we suggest the position of several functional domains including f-actin, synapsin I, ankyrin and spectrin self association sites. Analysis of deduced amino acid sequences indicated striking homology and similar structural characteristics of brain beta spectrin repeats beta 11 and beta 12 to globins. In vitro analysis has demonstrated that heme is capable of specific attachment to brain spectrin, suggesting possible new functions in electron transfer, oxygen binding, nitric oxide binding or heme scavenging.

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