Earticle

초록

영어

Variable glycosylation of antibodies occurs at Asn297 in the Fc region, specifically terminal galactosylation and sialylation. These variations may affect both pharmacokinetic behavior and effecter function, such as complement-dependant cytotoxicity (CDC). Among the variations in
N-glycosylation of the antibodies analyzed, highly galactosylated and sialylated antibodies demonstrated in vivo efficacy.
In this study, the degree of glycosylation of antibodies according to passages through the cell culture was compared in an attempt to find the condition showing greater in vivo efficacy of recombinant antibodies and so increasing their potential as therapeutic drugs. Suspension cultures of recombinant CHO cells were grown in protein-free media, and purification and analysis were performed using liquid chromatographic methods.
The results demonstrate that glycosylation can be changed by cell growth phase and passages through the cell culture. In early death phase during cell culture, the antibody was highly glycosylated, and as the subculture was repeated and prolonged in the same culture condition, glycosylation of the antibodies was advanced. In summary, the N-glycosylation rate (i.e. the percentage of N-glycan types such as G0, G1, and G2) can be controlled by experimental timing.

저자

• Seong-Min Kim [ Department of Bioscience&Biotechnology,sejong university ]
• Jang-hyeon Park [ Bio R&D C., Ltd. ]
• Duk-Jae Oh [ Department of Bioscience&Biotechnology,sejong university, Bio R&D C., Ltd. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576