Abstract
An immunoreactive analogue of erythrocyte spectrin has been purified from brain membranes. This protein co-sediments with and cross-links actin filaments, associates with spectrin-binding sites on erythrocyte membranes, and has been visualized by rotary shadowing as an extended, flexible rod. The brain spectrin comprises 3% of the total membrane protein, and may have a major role in mediating linkage of actin to membranes.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / metabolism
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Animals
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Brain Chemistry*
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Cell Membrane / analysis
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Erythrocyte Membrane / metabolism
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Humans
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Membrane Proteins / isolation & purification*
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Nerve Tissue Proteins / isolation & purification*
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Peptides / analysis
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Protein Conformation
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Spectrin / analogs & derivatives
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Spectrin / immunology
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Spectrin / isolation & purification*
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Swine
Substances
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Actins
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Membrane Proteins
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Nerve Tissue Proteins
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Peptides
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Spectrin