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Jing Zhai,Weishan Chang,Zhenzhen Zhai,Xingliang Ma,Lingling Yang,Jinfeng Ti,Daozhen Song,Shijun Fu,Dapeng Li 한국유전학회 2016 Genes & Genomics Vol.38 No.8
Few studies have attempted to characterize the pheasant (Phasianus colchicus) immunoglobulin Y (IgY) heavy chain constant region. In the present study, fragments of the pheasant IgY heavy chain constant region were cloned, analyzed, and expressed. The cross-reactivity of IgY or immunoglobulin G (IgG)s with antigens from other vertebrate species was determined using dot-enzymelinked immunosorbent assay and western blot analysis. Five peptides of the pheasant IgY heavy chain constant region were synthesized to determine its immunoregulatory activity in vitro. The IgY heavy chain constant region from pheasant showed the highest homology with that from chicken (71.2 %) and duck (49.1 %). Phylogenetic analysis for IgY showed that pheasant was closely related to chicken and duck than to any other analyzed vertebrate species. The rabbit anti-chicken IgG showed immunologic cross-reactivity with recombinant proteins of the pheasant IgY heavy chain constant region. Four peptides were able to induce significant up-regulation of interleukin (IL)-1b, IL-4, and interferon-c in chicken peripheral blood lymphocytes, suggesting a new role of avian IgY in immune regulation.
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Jie Sun,Jie Jiang,Xinyang Zhai,Shaoming Zhu,Zhenzhen Qu,Wei Yuan,Zhao Wang,Chun Wei 한국생물공학회 2019 Biotechnology and Bioprocess Engineering Vol.24 No.6
The large-scale production of functional recombinant lactoferrin has become a major goal because of its medicinal value and global demand. Secreting recombinant proteins into a culture medium offers a way to simplify protein purification and avoid toxicity from intracellularly accumulated materials. In this study, after 84 h of induction with methanol in a shaking flask, the recombinant bovine lactoferrin (rbLf) titer in the culture supernatant of the strain that integrated two copies of the rbLf gene was only 121.6 μg/L. A bottleneck might have existed in the folding and secretion pathways of rbLf. We then attempted to further improve the rbLf titer by overexpressing the transcription factor Hac1p and α-signal peptide-cutting protease Kex2p with different promoters. Results showed that the inducible coexpression of Hac1p and Kex2p linked with the 2A sequence improved the rbLf titer 5.0-fold (735.8 μg/L) after 84 h of induction with methanol. The maximal titer in a shaking flask was 1,150.5 μg/L after 120 h of induction. The rbLf titer achieved 35.6 mg/L in a 5 L fed-batch fermenter. Thus, Kex2 and Hac1 overexpression driven by methanol-induced promoter alleviated the bottleneck in the folding and secretion pathways and greatly improved the secretory expression of rbLf in Pichia pastoris.
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