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利用磺基异硫氰酸苯酯化学辅助方法鉴定磷酸化肽修饰位点

Identification of Phosphopeptide Modification Sites Based on Chemically-Assisted Method Using 4-Sulfophenyl Isothiocyanate Derivatization by Mass Spectrometry

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【Author】 CHEN Ping~ 1) , LI Shui-Ming~ 1) , LIU Yu~ 2) , LIU Zhong-Hua~ 1) , XIONG Ji-Xian~ 1) , SUN Ya-Lan~ 1) , CAO Rui~ 1) , LIANG Song-Ping~ 1) ( ~ 1) College of Life Sciences, Hunan Normal University, Changsha 410081, China; ~ 2) Xiangya Medical School, Central South University, Changsha 410078, China)

【机构】湖南师范大学生命科学学院；中南大学湘雅医学院；湖南师范大学生命科学学院长沙410081；长沙410081；长沙410078；

【摘要】利用MALDI-TOF质谱结合磺基异硫氰酸苯酯(SPITC)化学辅助的从头测序(de novosequencing)方法,将用固相金属离子亲和色谱(immobilized metal affinity chromatography,IMAC)选择性地从混合物中亲和提取的磷酸肽进行磷酸化位点测定,该方法只有肽键断裂产生的带C端的碎片离子系列(y+离子系列)出现在质谱图中,图谱背景清晰,信噪比高,单纯的y+片段离子系列使得谱图解析变得非常容易,对于多磷酸化肽的磷酸化位点,不需借助于任何软件,只需简单地计算两峰之间的分子量之差即可确定.更多还原

【Abstract】 Phosphorylated peptides have been detected and phosphorylation modified sites have been identified very sensitively by combining immobilized metal affinity chromatography (IMAC) affinity capture with chemically assisted de novo sequencing followed 4-sulfophenyl isothiocyanate (SPITC) derivatization by MALDI-TOF mass spectrometry. The N-terminal sulfonation of phosphopeptide by SPITC enhanced MALDI-TOF-PSD fragmentation signals and produced a spectrum containing only y~+ ions. This method facilitated de novo sequencing and spectrum interpretation. The characterization of phosphorylated sites can simply calculated from mass differences between the adjacent y-ion, and advanced software is not need.更多还原

【关键词】 SPITC；磷酸化位点；从头测序；质谱；
【Key words】 SPITC； phosphorylation sites； de novo sequencing； mass spectrometry；

【基金】国家自然科学基金资助项目No:39990600~~

【文献出处】中国生物化学与分子生物学报 ,Chinese Journal of Biochemistry and Molecular Biology , 编辑部邮箱 ,2006年07期

【分类号】Q75
【被引频次】2
【下载频次】164

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