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The S100‐b Protein: Tyrosine Residues Do Not Exhibit an Abnormal Fluorescence Spectrum
Author(s) -
Baudier Jacques,
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.tb08154.x
Subject(s) - tyrosine , fluorescence , s100 protein , protein subunit , chemistry , tryptophan , residue (chemistry) , biochemistry , microbiology and biotechnology , biology , amino acid , immunohistochemistry , gene , physics , immunology , quantum mechanics
The β subunit of the bovine brain S100‐b protein (ββ) lacks tryptophyl residue but contains one tyrosine. Our experiments show that this protein is characterized by a typical tyrosine fluorescence spectrum, with a maximum at 303 nm. Identical fluroescence properties were found for the rat brain S100‐b protein. Comparison with the fluorescence spectrum of the bovine brain S100‐a’ protein (α'β), which contains a tryptophan residue in the α’ subunit, enables us to demonstrate that the recent report describing an abnormal fluorescence spectrum for the bovine brain S100‐b protein may result from a contamination of the S100‐b by the S100‐α’ protein.