作者: Yongtao Liu , Mindi Zhao , Xuanzhen Pan , Youhe Gao
DOI: 10.1101/2020.03.07.978049
关键词:
摘要: Abstract The chemical modification of proteins refers to the covalent group reaction involved in their amino acid residues or chain ends which, turn, change molecular structure and function proteins. There are many types modifications human plasma proteome, such as phosphorylation, methylation, acetylation. In this study, two groups proteome at different age (old young) were used perform a comparison global modifications, determined by tandem mass spectrometry (MS/MS) combined with non-limiting identification algorithms. sulfhydryl cysteine A total 4 found have significant differences: succinylation phosphorylation (Cys, C) lysine (Lys, K) threonine (Thr, T) significantly higher old than young group, while carbamylation was lower group. Cysteine residue is an important for forming disulphide bonds maintaining protein. Differential cysteine-related sulfydryl may cause structural functional changes. Lysine basic acid, its will charge state protein, which affect summary, four protein substitutes be probabilities random generation passing grouping test. We speculate that there increase certain modified blood people changes those This one reasons why more likely risk age-related diseases, metabolic cerebral cardiovascular cancer.