Your browser doesn't support javascript.
loading
Characterization of human hybrid cell line, F2N78, through a comparison of culture performances and protein qualities.
Seo, Joon Serk; Min, Byung Sub; Kim, Yeon Jung; Cho, Jong Moon; Kwon, Gi-Seong; Lim, Byeong-Pil; Chang, Shin-Jae; Kim, Dong-Il.
Afiliação
  • Seo JS; Department of Biological Engineering, Inha University, Incheon, 22212, Korea.
  • Min BS; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Kim YJ; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Cho JM; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Kwon GS; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Lim BP; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Chang SJ; R&D Center, Celltrion, Incheon, 22014, Korea.
  • Kim DI; Department of Biological Engineering, Inha University, Incheon, 22212, Korea. kimdi@inha.ac.kr.
Biotechnol Lett ; 39(4): 501-509, 2017 Apr.
Article em En | MEDLINE | ID: mdl-28054185
OBJECTIVES: To evaluate the characteristics of a novel human cell line, F2N78, including growth performance, physicochemical properties, and biological activity via direct comparison with CHO cells. RESULTS: The culture performance and physicochemical properties of antibodies produced from F2N78 and CHO cells were compared. For charge variants, antibodies produced from F2N78 cells contained a greater acidic charge variants than CHO cells. Regarding main glycoforms, degree of galactosylation was 52% in CT-A produced from F2N78 cells compared to CHO cells (37%). For sialic acid forms, α-2,6-linked sialic acid and N-acetylneuraminic acid (NANA) residues were observed in antibodies produced from F2N78 cells. In contrast, only α-2,3 linked sialic acid forms were detected in antibodies produced from CHO cells, and NANA and N-glycolylneuraminic acid were detected. Hybrid structure and bisecting structure were only observed in F2N78 cells. CONCLUSIONS: F2N78 cells stably produced antibodies with human specific N-glycan. The novel expression system based on human cells may facilitate the development of an alternative host cell for production of recombinant proteins.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicosilação / Linhagem Celular / Anticorpos Monoclonais Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicosilação / Linhagem Celular / Anticorpos Monoclonais Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article