Properties of s100 protein studied by fluorescence methods
作者： Roberto D. Morero , Gregorio Weber
DOI: 10.1016/0167-4838(82)90053-X
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摘要: The intrinsic fluorescence of the S100 protein, due to both tyrosine and tryptophan, increases several-fold, in reversible fashion, solutions at pH 3.0 comparison with neutral molecule. study rotational diffusion photo-conjugates l-azidonaphthalene-5-sulfonate as a function pH, concentration-dependence polarization electrophoretic patterns indicate that protein unfolding without dissociation into subunits takes place region 4-3.4 is complete μM 2.9. Anionic binding sites, probably connected arginine residues, can be detected acid solutions, indicated by 30-fold increase efficiency added anilinonaphthalene sulfonate 3.4, compared pH. At 3.4 transferred reversibly an isobutanol or pentanol phase, not only addition sodium p-toluenesulfonate, which effect observed for other globular proteins, but calcium chloride magnesium well, specific related this protein.
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