The University of Osaka · 생화학·유전·분자생물학
Kazuhito Fujiyama 교수의 연구실은 식물에서의 약물 단백질 생산을 위한 게노믹 및 게노믹 공학 기반의 생물학적 기술 개발에 주력하고 있습니다. 특히 식물의 N-결합 접합당단백질의 당사슬 구조를 제어하여 인간 치료용 단백질의 안정성과 면역원성 저감을 도모하는 연구를 수행하고 있으며, 고유한 당구조를 갖는 식물 단백질의 구조 분석과 변형 기술이 핵심입니다. 또한, 라이스(쌀)와 페퍼 등 식물 시스템을 활용한 외래 단백질의 효율적 발현 및 당구조 분석을 통해 바이오의약품 생산의 실용화를 추구하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
We have isolated, cloned and characterized three cDNAs and two genomic DNAs corresponding to the mRNAs and genes for the horseradish (Armoracia rusticana) peroxidase isoenzyme C (HPR C). The amino acid sequence of HRP C1, deduced from the nucleotide sequence of one of the cDNA clone, pSK1, contained the same primary sequence as that of the purified enzyme established by Welinder [FEBS Lett. 72, 19-23 (1976)] with additional sequences at the N and C terminal. All three inserts in the cDNA clones,
For the production of therapeutic proteins in plants, the presence of β1,2-xylose and core α1,3-fucose on plants' N-glycan structures has been debated for their antigenic activity. In this study, RNA interference (RNAi) technology was used to down-regulate the endogenous N-acetylglucosaminyltransferase I (GNTI) expression in Nicotiana benthamiana. One glyco-engineered line (NbGNTI-RNAi) showed a strong reduction of plant-specific N-glycans, with the result that as much as 90.9% of the total N-gl
Human lactoferrin was produced in genetically engineered rice. N-linked glycan structures of recombinant human lactoferrin were determined. The oligosaccharides liberated by hydrazinolysis were labeled with 2-aminopyridine (PA). The PA-labeled glycans were purified by reverse-phase and size-fractionation HPLCs. The structures of these glycans were identified by HPLC, exoglycosidase digestion, and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The glycan
