| Summary: | 碩士 === 國立陽明大學 === 生化暨分子生物研究所 === 100 === Protein posttranslational modification is important in either current biology studies or clinical biomarker discovery. Most of analytical strategies were limited to only identifying specific modification and relied on cataloging analyses. However, there is not a differential tool to meet the requirement.
In chapter II, casein was used to test our differential analysis platform. In vitro dephosphorylation by alkaline phosphatase was applied to produce reference protein in a paired analysis. After data processing by our in-house programs, known phosphorylation sites in caseins can be successfully screened using our differential analyses platform.
In chapter III, we used this newly developed platform to screen glycation on albumin. We indeed discovered difference expressed glycation on albumin from diabetic patient based on their ion cluster patterns indicating differential expression after MS analyses. It is noteworthy that two novel in vivo sites have been identified accordingly. While examining the MS data, we serendipitously found out that glycated peptides appear to pick up a third 18O atom during the sample preparation procedure.
In summary, we have developed a differential analysis that can target more than two types of protein modifications including phosphopeptides and glycated peptides. With the development of informatics tools for MS/MS interpretation, we should be able to identify more differentially expressed protein modifications.
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