Earticle

초록

영어

Glycosylation is one of the most abundant protein modifications and plays an important role in many specific biological functions. Various investigations concerning quantitative glycan analysis have been performed because of the importance of the oligosaccharide moiety on glycoproteins in biological systems. There are several technologies in quantifying the N-linked glycans in an effective manner such as 13CH3I and QUIBL within vitro isotopic and isobaric labeling. Endo-β-N-acetylglucosaminidase (Endo-M) hydrolyzes the diacetylchitobiose core of the N-linked glycans bound to the asparagines of various glycoproteins and transfers the intact complex oligosaccharides to suitable acceptors. The transglycosylation activity of Endo-M is dependent on the several experimental parameters such as pH and temperature with the acceptors. As an alternative quantification method of N-linked glycans, we report a chemoenzymatic isotope labeling of fully sialylated N-linked glycans by a transglycosylation reaction using Endo-M and glucose as acceptors. The results provide the use of a quantitative technology for fully sialylated N-linked glycans in biological systems such as the processes of diseases and development of cells.

저자

• Su-Hee Jeong [ Department of Chemistry, Changwon National University ]
• Seongha Park [ Department of Chemistry, Changwon National University ]
• Yong-Ill Lee [ Department of Chemistry, Changwon National University ]
• Jae-Min Lim [ Department of Chemistry, Changwon National University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614