Faculty Research 1990 - 1999

Title

The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences [published errata appear in Brain Res Mol Brain Res 1993 Oct;20(1-2):179 and 1994 Jan;21(1-2):181 and 1995 May;30(1):176]

Document Type

Article

Publication Date

1993

Keywords

Amino-Acid-Sequence, Animal, Base-Sequence, Binding-Sites, Brain-Chemistry, Carrier-Proteins: ge, me, Comparative-Study, Consensus-Sequence, DNA: ge, Globin: ge, Hemin: me, Mice, Mice-Inbred-BALB-C, Microfilament-Proteins: ge, me, Molecular-Sequence-Data, Multigene-Family, Nerve-Tissue-Proteins: ge, me, Sequence-Alignment, Sequence-Homology-Amino-Acid, Spectrin: ge, me, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S

JAX Source

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

Grant

HL29305/HL/NHLBI, NS19357/NS/NINDS, NS26536/NS/NINDS

Abstract

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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