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  • 09월 05일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제120회 대한화학회 학술발표회, 총회 및 기기전시회 안내 On-line proteolysis and glycopeptide enrichment using dual micro-scale porous polymer membrane enzyme reactor (μPPMER) and nanoflow liquid chromatography-tandem mass spectrometry

등록일
2017년 8월 22일 15시 52분 41초
접수번호
3020
발표코드
ANAL1.O-23 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 10시 : 05분
발표형식
구두발표
발표분야
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
공동저자
JoonSeon Yang, Juan Qiao1, Liping Zhao2, Li Qi2,*, Myeong Hee Moon*
Department of Chemistry, Yonsei University, Korea
1Beijing National Laboratory for Molecular Sciences; Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Acedemy of Sciences, Chile
2Beijing National Laboratory for Molecular Sciences; Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Acedemy of Sciences, China
※ 국외소속으로 등록된 저자의 승인여부는 최소 3일이내 발표자 email로 알려드립니다.
승인 3건
N-glycosylation is a type of glycosylation that occurs when glycans are attached to the nitrogen atom of asparagine (asn, N). It is important to analyze N-glycoproteins in biological samples as they play essential roles in protein folding or signaling process. However, analysis of glycoproteins from glycopeptides by shotgun analysis can be time-consuming and sample loss is inevitable during pre-treatments. Therefore, to overcome such problems, dual micro-scale thermo-sensitive porous polymer membrane enzyme reactors (μPPMER) has been utilized for on-line proteolysis, followed by enrichment of glycopeptides prior to nanoflow liquid chromatography-tandem mass spectrometry (nLC-ESI-MS/MS). A thermo-responsive porous polymer membrane (T-PPM) was synthesized by coating PS-co-MAn-NIPAM polymer on bare nylon membrane and its characterization was conducted by SEM. Trypsin and lectin were immobilized on the coated membrane for proteolysis and glycopeptide capture, respectively, and each of membrane was inserted in μPPMER module. Dual μPPMER modules were connected to nLC-ESI-MS/MS system for on-line analysis and efficiency in glycopeptides enrichment selectivity under various temperatures were evaluated. In addition, glycoproteins from human plasma and urine samples were analyzed using on-line dual PPMER module in the most optimized condition for glycopeptide enrichment.

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