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邻苯二甲醛修饰法探测中华猕猴桃蛋白酶在胍溶液中活性部位的构象变化; Detection of ConFormational Changes at the Active Site of Actinidin in GuHCl Solutions by o-Phthaldehyde ModiFication
颜青 ; 林青松 ; 颜思旭
1997
关键词Actinidin o-Phthaldehyde Chemical modiFication ConFormation of active site
英文摘要The thiol group and amino group at the active site of actinidin were modiFied by o-phthaldehyde to Form a Fluorescence group with excitation and emission wavelength maxima at 345 um and 416 nm respectively.The Fluorescence group was then used to probe the conFormational changes of the modiFied enzyme in guanidine hydrochloride (GuHCl) solution.Results were compared with the changes of activity as well as Fluorescence and CD spectra of unmodiFied actinidin in GuHCl sloutions.It is shown that the conFormational changes of the enayme active site parallel the enzyme inactivation, and both of them precede the conFormatvonal changes of the enzyme as a whole revealed by Fluorescence and CD spectra.; 国家自然科学基金
语种zh_CN
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/123829]  
专题医学院-已发表论文
推荐引用方式
GB/T 7714
颜青,林青松,颜思旭. 邻苯二甲醛修饰法探测中华猕猴桃蛋白酶在胍溶液中活性部位的构象变化, Detection of ConFormational Changes at the Active Site of Actinidin in GuHCl Solutions by o-Phthaldehyde ModiFication[J],1997.
APA 颜青,林青松,&颜思旭.(1997).邻苯二甲醛修饰法探测中华猕猴桃蛋白酶在胍溶液中活性部位的构象变化..
MLA 颜青,et al."邻苯二甲醛修饰法探测中华猕猴桃蛋白酶在胍溶液中活性部位的构象变化".(1997).
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