The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences.
Details
Serval ID
serval:BIB_7F50FCC0F943
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences.
Journal
Brain Research. Molecular Brain Research
ISSN
0169-328X (Print)
ISSN-L
0169-328X
Publication state
Published
Issued date
1993
Volume
18
Number
1-2
Pages
87-99
Language
english
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.
Keywords
Actins/metabolism, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Brain Chemistry, Carrier Proteins/genetics, Carrier Proteins/metabolism, Consensus Sequence, DNA/genetics, Globins/genetics, Hemin/metabolism, Mice, Mice, Inbred BALB C, Microfilament Proteins/genetics, Microfilament Proteins/metabolism, Molecular Sequence Data, Multigene Family, Nerve Tissue Proteins/genetics, Nerve Tissue Proteins/metabolism, Sequence Alignment, Sequence Homology, Amino Acid, Spectrin/genetics, Spectrin/metabolism
Pubmed
Web of science
Create date
24/01/2008 15:35
Last modification date
20/08/2019 15:40
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