摘要
Biliary protein was isolated and purified by ammonium sulfate fraction ation and Sephadex G-75 gel filtration column chromatography. FTIR showed that w as a glycoprotein. Its molecular weight was determined as 34.7 kD by MS. The int eraction between Mg2+ and biliary protein was studied by fluorescence spectrosco py 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.
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.
出处
《无机化学学报》
SCIE
CAS
CSCD
北大核心
2005年第3期413-416,共4页
Chinese Journal of Inorganic Chemistry
基金
国家自然科学基金资助项目(No.20031010
20371001)
