期刊
CHINESE SCIENCE BULLETIN
卷 47, 期 7, 页码 538-542出版社
SCIENCE CHINA PRESS
DOI: 10.1360/02tb9124
关键词
hemoglobin (Hb); serum albumin (SA); nicotine; spectroscopic studies
The interactions of nicotine and Hb/SA were studied in vitro by UV/Vis, fluorescence, H-1 NMR and FT-IR spectroscopies. The UV/Vis absorbance of Hb/SA (200 nm) shifted to red and decreased gradually with the addition of nicotine, indicating that the protein conformational change resulted from the chemical interaction. With increasing nicotine concentration, incubation of SA with nicotine caused the quenching of fluorescence typical of protein tryptophan residues, which meant that the vicinity of the tryptophan residues of SA was changed because of nicotine. FT-IR spectra showed that alpha-helix component of Hb/SA decreased, turn and beta-structure components of Hb/SA increased in the presence of nicotine. In the H-1 NMR spectra of nicotine, all proton peaks on pyrrolidinyl ring moved to downfield and the resonance emanating from nicotine was preferentially broadened while the concentration of Hb/SA increased. All these results indicate that nicotine and Hb/SA in vitro interact on each other, forming a new complex and inducing the protein conformational change.
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