지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
오류제보하기
Protein glycation is vital to aging and disease. However, glycated proteins are low-abundant in plasma, rendering them difficult to identify using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Many studies have analyzed glycated peptides with high reproducibility. Here, glycated peptides in human serum were analyzed by LC-MS/MS using data-dependent acquisition (DDA) and parallel reaction monitoring (PRM). Boronic acid (BA) enrichment of in vitro glycated human serum peptides was performed. BA enrichment identified the most glycated peptides, and the glycated peptides of the more diversified proteins, excluding albumin, were analyzed. In PRM, glycated albumin PSMs were the most common, and this method exhibited the best reproducibility. The results of this study could help compare methods for identifying glycation-related biomarkers.
목차
Abstract
1. Introduction
2. Experimental
3. Results and Discussion
4. Conclusions
References
참고문헌 (28)
참고문헌 신청
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C.-S. Kim, S. Park, and J. Kim, J. Exerc. Nutr. Biochem., 21, 55-61 (2017).
K. Byun, Y. Yoo, M. Son, J. Lee, G.-B. Jeong, Y. M. Park, G. H. Salekdeh, and B. Lee, Pharmacol. Ther., 177, 44-55 (2017).
G. Münch, J. Thome, P. Foley, R. Schinzel, and P. Riederer, Brain Res. Brain Res. Rev., 23, 134-143 (1997).
H. Vlassara and J. Uribarri, Curr. Diab. Rep., 14, Article Number 453 (2014).
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