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Bovine Brain S100 Proteins: Separation and Characterization of a New S100 Protein Species
Author(s) -
Baudier Jacques,
Mandel Paul,
Gérard Dominique
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb12664.x
Subject(s) - sodium dodecyl sulfate , chemistry , tryptophan , polyacrylamide gel electrophoresis , gel electrophoresis , urea , fluorescence , chromatography , biochemistry , amino acid , physics , quantum mechanics , enzyme
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 anew tryptophan‐containing S100 protein called S100a′, which exhibits, as S100a and S100b, the properties of a Ca 2+ binding protein.