Document Detail

The identification and sequence of the actin-binding domain of human red blood cell beta-spectrin.
MedLine Citation:
PMID:  2365703     Owner:  NLM     Status:  MEDLINE    
The junctions of the red blood cell membrane skeleton are formed by interactions between spectrin and actin protofilaments. A spectrin tryptic peptide of 16.5-kDa apparent molecular mass (based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis) which binds to F-actin in cosedimentation experiments has been identified. The peptide has been partially purified by gel filtration, anion-, and cation exchange chromatography. Intact spectrin heterodimer causes half-maximal inhibition of the 16.5-kDa peptide/F-actin interaction at a concentration of 5 microM. Comparison of the two-dimensional iodopeptide maps of the 16.5-kDa peptide with maps of alpha- and beta-spectrin, demonstrate that the peptide is generated from the beta subunit. It shows no significant relationship to the peptide maps of the beta-spectrin domains I-IV. Protein sequencing indicated that this actin-binding domain represents a stretch of amino acids at the N terminus of the beta subunit from alanine 47 probably through lysine 186. The sequence derived molecular weight of this actin-binding domain is 16,290 g/mol. The sequence presented represents the region of greatest homology among the spectrin supergene family (spectrin, dystrophin, alpha-actinin).
A M Karinch; W E Zimmer; S R Goodman
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  265     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1990 Jul 
Date Detail:
Created Date:  1990-08-14     Completed Date:  1990-08-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  11833-40     Citation Subset:  IM    
Department of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Hershey, Pennsylvania 17033.
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MeSH Terms
Actins / isolation & purification,  metabolism*
Amino Acid Sequence
Binding Sites
Binding, Competitive
Chromatography, Gel
Erythrocytes / metabolism
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
Muscles / metabolism
Peptide Fragments / isolation & purification,  metabolism
Sequence Homology, Nucleic Acid
Spectrin / genetics,  isolation & purification,  metabolism*
Grant Support
Reg. No./Substance:
0/Actins; 0/Macromolecular Substances; 0/Peptide Fragments; 12634-43-4/Spectrin; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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