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    
Abstract/OtherAbstract:
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).
Authors:
A M Karinch; W E Zimmer; S R Goodman
Related Documents :
15250723 - Propeller-type parallel-stranded g-quadruplexes in the human c-myc promoter.
24059223 - Pharmacophore-based 3d qsar and molecular docking studies to identify new non-peptidic ...
6401783 - Biochemical characterization of ia antigens. characterization of a 22,000-dalton a delt...
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    
Affiliation:
Department of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Hershey, Pennsylvania 17033.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Actins / isolation & purification,  metabolism*
Amino Acid Sequence
Animals
Binding Sites
Binding, Competitive
Chromatography, Gel
Erythrocytes / metabolism
Humans
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
Muscles / metabolism
Peptide Fragments / isolation & purification,  metabolism
Rabbits
Sequence Homology, Nucleic Acid
Spectrin / genetics,  isolation & purification,  metabolism*
Trypsin
Grant Support
ID/Acronym/Agency:
HL-26059/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Macromolecular Substances; 0/Peptide Fragments; 12634-43-4/Spectrin; EC 3.4.21.4/Trypsin

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


Previous Document:  Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl termi...
Next Document:  Pasteurella multocida toxin, a potent mitogen, stimulates protein kinase C-dependent and -independen...