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Interaction of Nicotine and Bovine Serum Albumin


  The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption. fluorescence. and ~1H NMR methods. With the addition of nicotine. the absorption band of BSA at about 210.nm decreased gradually, moved to longer wavelengths. and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The ~1H NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA s high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.……   
[关键词]:Nicotine;BSA;UV absorption;fluorescence;H NMR.
[文献类型]:期刊
[文献出处]: 《Chinese Chemical Letters2000年03期