| The identification and sequence of the actin-binding domain of human red blood cell beta-spectrin. | |
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MedLine Citation:
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PMID: 2365703 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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). |
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Authors:
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A M Karinch; W E Zimmer; S R Goodman |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 265 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1990 Jul |
Date Detail:
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Created Date: 1990-08-14 Completed Date: 1990-08-14 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 11833-40 Citation Subset: IM |
Affiliation:
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Department of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Hershey, Pennsylvania 17033. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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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:
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HL-26059/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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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
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