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

• 来源期刊: 高等学校化学研究（英文版）
• 年，卷（期）: 2019,（3）
• 页码范围: 377-381
• 页数: 5页
• 语种: 英文
• DOI: 10.1007/s40242-019-8377-1

摘要

Talin protein was partially purified from humaan 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 ruth capillary reverse-phase high-perfonnance liquid chromatography was used to analyze the enriched peptides.Specifically,four peptides containing diglycyl-Lys remnants from talin,nanely,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 the relationship between ubiquitination modification of talin and its biological activity in colorectal cancer tissues with different pathological processes.