Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

查看全文 作　　者：WANG [1]Ke;QIAO [1]Lu;LI [2]Xiaoou;LI [1]Shimeng;WANG [1]Yimin;XU [1]Xuesong;HE [1]Chengyan;FANG [1]Ling 机构地区：[1]China-Japan Union Hospital,Jilin University,Changchun 130033,P.R.China;[2]Tumor Hospital of Jilin Province,Changchun 130012,P.R.China 出　　处：《Chemical Research in Chinese Universities》索引2019年第35卷第3期,共5页 基　　金：the Science and Technology Department of Jilin Province,China(No.20150414015GH);the National Natural Science Foundation of China(Nos.81572082, 81472454). 摘　　要：Talin protein was partially purified from human colorectal carcinoma tissues, which was subject to tryptic digestion. Immunoaffinity precipitation with specific antibodies that recognize diglycyl-lysine(Lys) remnants from tryptic digestion of ubiquitinated peptides was used to enrich ubiquitinated sites in talin. Mass spectrometry coupled with capillary reverse-phase high-performance liquid chromatography was used to analyze tlie enriched peptides. Specifically, four peptides containing diglycyl-Lys remnants from talin, namely, TAK(ub)VLVEDTK, QQQYK(ub) FLPSELRDEH, K(ub)STVLQQQYNR, and EGILK(ub)TAK can be determined using mass spectrometric data. This study provides an analytical method for further study in tlie relationship between ubiquitination modification of talin and its biological activity in colorectal cancer tissues with different pathological processes. 关 键 词：TALIN UBIQUITINATION COLORECTAL carcinoma Mass SPECTROMETRY