Therapeutic proteins play an increasingly important role in the pharmaceutical industry. Glycosylation is a very critical modification of therapeutic proteins, known to significantly modulate yield, bioactivity, solubility, immunogenicity and efficacy. Most biotherapeutic proteins developed to date have been produced using the mammalian model. Although mammalian system can produce glycosylation similar to human, they also produce non-human glycosylation that can cause immune responses and safety issue. Firstly, we explored difference of glycosylation between human and mouse to design glycan-humanized mouse model. We selectively enriched glycans from blood cell (red blood cell and white blood cell) membrane and analyzed them by porous graphitized carbon (PGC) based nano-LC/MS which enables to confirm not only glycan composition but also structure isomer. Hundreds of glycan structures were directly detected by accurate mass and structurally elucidated by MS/MS, revealing the species-specific structure. These results could be targets for new signatures distinguishing the species and the beginning for design of glycan-humanized mouse model.
저자
Dan Bi Park [ Chungnam National University, Asia-Pacific Glycomics Reference Site, 99 Daehak-ro, Yuseong-gu, Daejeon, 34134, Korea ]
Sumin Kim [ Chungnam National University, Asia-Pacific Glycomics Reference Site, 99 Daehak-ro, Yuseong-gu, Daejeon, 34134, Korea ]
Hyun Joo An [ Chungnam National University, Asia-Pacific Glycomics Reference Site, 99 Daehak-ro, Yuseong-gu, Daejeon, 34134, Korea ]
본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.