The complete amino acid sequence for brain β spectrin (β fodrin)

relationship to globin sequences

Yupo Ma, Warren E. Zimmer, Beat M. Riederer, Steven Goodman

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

The amino acid sequence of mouse brain β spectrin (β fodrin), deduced from the nucleotide sequence of complementary DNA clones, reveals that this non-erythroid β spectrin comprises 2363 residues, with a molecular weight of 274,449 Da. Brain β 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 β spectrin repeats β11 and β12 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.

Original languageEnglish (US)
Pages (from-to)87-99
Number of pages13
JournalMolecular Brain Research
Volume18
Issue number1-2
DOIs
StatePublished - Jan 1 1993
Externally publishedYes

Fingerprint

Spectrin
Globins
Amino Acid Sequence
Brain
Heme
Synapsins
Ankyrins
Protein Sequence Analysis
fodrin
Actins
Nitric Oxide
Complementary DNA
Clone Cells
Molecular Weight
Electrons
Oxygen

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cellular and Molecular Neuroscience

Cite this

The complete amino acid sequence for brain β spectrin (β fodrin) : relationship to globin sequences. / Ma, Yupo; Zimmer, Warren E.; Riederer, Beat M.; Goodman, Steven.

In: Molecular Brain Research, Vol. 18, No. 1-2, 01.01.1993, p. 87-99.

Research output: Contribution to journalArticle

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