Faculty Research 1990 - 1999
The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences.
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, Genes-Reiterated, Globin: ge, Hemin: me, Mice, Mice-Inbred-BALB-C, Microfilament-Proteins: ge, me, Molecular-Sequence-Data, 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
First Page
87
Last Page
99
JAX Source
Brain Res Mol Brain Res 1993 Apr;18(1-2):87-99
Grant
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.
Recommended Citation
Ma Y,
Zimmer WE,
Riederer BM,
Goodman SR,
Bloom ML,
Barker JE.
The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences. Brain Res Mol Brain Res 1993 Apr;18(1-2):87-99