Biliary protein was isolated and purified by ammonium sulfate fractionation and Sephadex G-75 gel filtration column chromatography. FTIR showed that was a glycoprotein. Its molecular weight was determined as 34.7 kD by MS. The interaction between Mg2+ and biliary protein was studied by fluorescence spectroscopy and UV-Visible spectroscopy. The result showed the quenching mechanism of the combination of Mg2+ with biliary protein was a static quenching procedure. The protein underwent conformation changing and unfolding, more hydrophobic residues would be exposed to solvents after the Mg2+ was added.
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