Abstract
Three S100 protein species (S100a, S100b, S100a') have been purified from bovine brain using a modification of standard preparative methods. A higher yield for each protein was obtained at the last separation step. Characterization by urea/sodium dodecyl sulfate/polyacrylamide gel electrophoresis, UV absorption spectra, and fluorescence parameters provided evidence of a new tryptophan-containing S100 protein called S100a', which exhibits, as S100a and S100b, the properties of a Ca2+ binding protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Biomarkers*
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Brain Chemistry*
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Calcium
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Cattle
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Chromatography, Gel
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Chromatography, Ion Exchange
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Immunodiffusion
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Molecular Weight
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Nerve Growth Factors
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Nerve Tissue Proteins / isolation & purification*
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Peptide Fragments / analysis
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S100 Calcium Binding Protein beta Subunit
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S100 Proteins / isolation & purification*
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Spectrophotometry, Ultraviolet
Substances
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Biomarkers
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Nerve Growth Factors
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Nerve Tissue Proteins
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Peptide Fragments
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S-100 calcium-binding protein alpha subunit
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S100 Calcium Binding Protein beta Subunit
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S100 Proteins
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Calcium