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Updated: Aug 19, 2026

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
The S100-b protein: tyrosine residues do not exhibit an abnormal fluorescence spectrum
Abstract:
The beta subunit of the bovine brain S100-b protein (beta beta) 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 fluorescence properties were found for the rat brain S100-b protein. Comparison with the fluorescence spectrum of the bovine brain S100-a' protein (alpha'beta), which contains a tryptophan residue in the alpha' 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-a' protein.
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