Abstract
In this study, two groups of human plasma proteome at different age groups (old and young) were used to perform a comparison of global chemical modifications, as determined by tandem mass spectrometry (MS/MS) combined with non-limiting modification identification algorithms. The sulfhydryl in the cysteine A total of 4 molecular modifications were found to have significant differences passing random grouping tests: the succinylation and phosphorylation modification of cysteine (Cys, C) and the modification of lysine (Lys, K) with threonine (Thr, T) were significantly higher in the old group than in the young group, while the carbamylation of lysine was lower in the young group. We speculate that there is an increase in certain modified proteins in the blood of the old people which, in turn, changes the function of those proteins. This change may be one of the reasons why old people are more likely than young people to be at risk for age-related diseases, such as metabolic diseases, cerebral and cardiovascular diseases, and cancer.
Highlights
In this study, two groups of human plasma proteome at different age groups were used to perform a comparison of global chemical modifications, as determined by tandem mass spectrometry (MS/MS) combined with non-limiting modification identification algorithms
The main types of chemical modifications related to proteins are as follows: (1) Post-translational modifications (PTMs) refer to the chemical modification of a protein after translation[4]
Based on the importance of chemical modifications in the human plasma proteome, this study attempted to compare the differences in the global chemical modification levels of the plasma proteome at two different age groups, as determined by high-resolution tandem mass spectrometry combined with non-limiting modification identification (Open-pFind)
Summary
Two groups of human plasma proteome at different age groups (old and young) were used to perform a comparison of global chemical modifications, as determined by tandem mass spectrometry (MS/MS) combined with non-limiting modification identification algorithms. Acid substitution refers to the change in protein properties and functions caused by the substitution of amino acids in the protein side-chain by other kinds of amino acids These changes are the types of modifications that significantly affect protein function. Based on the importance of chemical modifications in the human plasma proteome, this study attempted to compare the differences in the global chemical modification levels of the plasma proteome at two different age groups, as determined by high-resolution tandem mass spectrometry combined with non-limiting modification identification (Open-pFind)
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