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  • 03월 02일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural Elucidation of Mouse Brain Glycoslyation using Nano-LC/MS/MS

등록일
2016년 2월 18일 15시 20분 28초
접수번호
3111
발표코드
ANAL2.O-16 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 10시 : 32분
발표형식
구두발표
발표분야
분석화학 - 젊은 분석화학자의 구두 발표 II (Oral Presentation of Young Analytical Chemists II)
저자 및
공동저자
박단비, 안현주*
충남대학교 분석과학기술대학원, Korea
Glycosylation represents common post-translational modification and plays primary roles in many neurological processes including development, nerve formation, transmission of the nervous system. It is well known that brain glycosylation correlates with neurodegenerative disease such as Alzheimer’s and Parkinson’s disease. Thus brain glycan characterization is positively necessary field. However, there are few structural studies on brain glycosylation because of glycan structures are complicated by the existence of stereoisomer, various linkage combinations, and branching. In the present study, tandem mass spectrometry (MS) under conditions of collision-induced dissociation (CID) was utilized to characterize N-glycan extracted from mouse brain tissue. CID is the most commonly used method for fragmenting glycan ions and generated mainly glycosidic B/Y cleavages of the glycans moieties. We comprehensively profiled the hundreds of glycan and confirmed over 80 N-glycan structures in mouse brain. Multiply fucosylation is significant structural feature observed on mouse brain glycans. The location of these fucose decorations was determined by MS/MS spectra were screened for diagnostic fragment ions at m/z 512.20 (Hex1HexNAc1Fuc1, associated with antennary fucosylation), and 1057.39 (Hex3HexNAc2Fuc1, associated with core fucosylation). Also, we observed several glycan motifs such as sulfation and glucuronidation by both accurate mass MS and MS/MS diagnostic fragment ions. Sulfation and glucuronidation have been associated with cell adhesion molecules, playing an important regulatory role in memory formation. The present data will be useful for structural and functional studies of mouse brain glycosylation.

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