透明质酸酶的色氨酸残基修饰与荧光光谱研究  

Studies on Tryptophan Residue Modification and Fluorescence Spectrum of Hyaluronidase

作　　者：滕利荣[1] 初宇卓[1] 张晓萍[1] 王静[1] 韩松[1] 于笑坤[1] 刘兰英[1] 

机构地区：[1]吉林大学生命科学学院,长春130023

出　　处：《高等学校化学学报》2005年第9期1662-1664,共3页Chemical Journal of Chinese Universities

基　　金：吉林大学2004年学生科技创新基金资助.

摘　　要：Tryptophan residues in Hyaluronidase(HAase) were modified by N-bromosuccinimide(NBS). The results indicated that there were eleven tryptophan residues in HAase and one of them was exposed, which was proved to be essential for the activity of the enzyme. The study on fluorescence quenching of HAase showed that KI could not quench all of the fluorescence from Trp residues in HAase . Acrylamide(Acr), a polarized quencher without electronic charge, could quench almost all of the fluorescence from Trp residues in HAase . The collisional quenching constants(K-D) of HAase at different concentrations of Acr were calculated in terms of Stern-Volmer equation. The results implied that some of Trp residues were buried in the interior of HAase, and the Trp residue on the surface of HAase was not located in the hydrophobic pocket.Tryptophan residues in Hyaluronidase（HAase） were modified by N-bromosuccinimide（NBS）. The results indicated that there were eleven tryptophan residues in HAase and one of them was exposed, which was proved to be essential for the activity of the enzyme. The study on fluorescence quenching of HAase showed that KI could not quench all of the fluorescence from Trp residues in HAase . Acrylamide（ Acr）, a polarized quencher without electronic charge, could quench almost all of the fluorescence from Trp residues in HAase. The collisional quenching constants（KD） of HAase at different concentrations of Acr were calculated in terms of Stem-Volmer equation. The results implied that some of Trp residues were buried in the interior of HAase, and the Trp residue on the surface of HAase was not located in the hydrophobic pocket.

关 键 词：透明质酸酶 色氨酸残基 化学修饰 荧光猝灭 

分 类 号：Q556[生物学—生物化学]