초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 02월 28일 19시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제111회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Targeted Proteomics; Glycan-Targeting Serial Affinity Chromatography

2013년 2월 28일 12시 08분 27초
ANAL.P-566 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 17일 (수요일) 16:00~19:00
저자 및
조원련*, 민철현1
원광대학교 생명나노화학부, Korea
1원광대학교 화학과, Korea
Glycan-targeting affinity chromatography systems are becoming increasingly important as tools in the purification, enrichment, and identification of glycoproteins. The great advantage of this strategy is that immobilized lectin and antibody selectors allow specific glycan structures to be matched with a particular protein. A problem with single column affinity chromatography is how to obtain information on glycan diversity within the oligosaccharide portions of captured glycoproteins. Although all the glycoprotein species bearing a particular glycan feature will be captured by an affinity column, there is no way of knowing whether the ligand being targeted appears alone or co-resides with a series of other glycan features in the same oligosaccharide conjugate. The utility of serial affinity columns was examined in determining whether individual glycan structures appear alone or together with other glycans in specific proteins. Serial affinity chromatography (SAC) can be a valuable tool in recognizing diversity in protein glycosylation, especially when the order of columns in the SAC series is varied. Two clear types of diversity were recognized. One is the independent occurrence of different affinity targetable glycan features in the same glycoprotein. The second is the case in which multiple targetable glycan features were co-resident in the same glycoprotein. The great advantage of this method is that it couples easily with current methods used in glycoproeomics.