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


Autoria(s): Ma Y.; Zimmer W.E.; Riederer B.M.; Bloom M.L.; Barker J.E.; Goodman S.M.; Goodman S.R.
Data(s)

1993

Resumo

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.

Identificador

http://serval.unil.ch/?id=serval:BIB_7F50FCC0F943

isbn:0169-328X (Print)

pmid:8479293

doi:10.1016/0169-328X(93)90176-P

isiid:A1993KU59000009

Idioma(s)

en

Fonte

Brain Research. Molecular Brain Research, vol. 18, no. 1-2, pp. 87-99

Palavras-Chave #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
Tipo

info:eu-repo/semantics/article

article