Expression of coxsackievirus and adenovirus receptor (CAR)-Fc fusion protein in Pichia pastoris and characterization of its anti-coxsackievirus activity

2013 ◽  
Vol 164 (4) ◽  
pp. 461-468 ◽  
Author(s):  
Kebin Zhang ◽  
Hua Yu ◽  
Wei Xie ◽  
Zihui Xu ◽  
Shiwen Zhou ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Fc Fusion Protein ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

Purification and characterization of human IL-10/Fc fusion protein expressed in Pichia pastoris

2012 ◽  
Vol 83 (2) ◽  
pp. 152-156 ◽  
Author(s):  
Yugang Guo ◽  
Wenyao Kang ◽  
Yongjun Zhong ◽  
Rui Li ◽  
Guangwei Li ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Purification And Characterization ◽  
Fc Fusion Protein

Preparation and characterization of a VEGF-Fc fusion protein matrix for enhancing HUVEC growth

2012 ◽  
Vol 34 (9) ◽  
pp. 1765-1771 ◽  
Author(s):  
Meihua Yu ◽  
Fengyi Du ◽  
Hirohiko Ise ◽  
Wei Zhao ◽  
Yan Zhang ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protein Matrix ◽  
Fc Fusion Protein

In-fusion expression and characterization of β-xylanase and β-1,3-1,4-glucanase in Pichia pastoris

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Jiayun Qiao ◽  
Yunhe Cao
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Fusion Protein ◽  
Fusion Expression ◽  
Chimeric Genes ◽  
Fusion Enzyme ◽  
Fusion Enzymes ◽  
Aspergillus Sulphureus

AbstractTwo chimeric genes, XynA-Bs-Glu-1 and XynA-Bs-Glu-2, encoding Aspergillus sulphureus β-xylanase (XynA, 26 kDa) and Bacillus subtilis β-1,3-1,4-glucanase (Bs-Glu, 30 kDa), were constructed via in-fusion by different linkers and expressed successfully in Pichia pastoris. The fusion protein (50 kDa) exhibited both β-xylanase and β-1,3-1,4-glucanase activities. Compared with parental enzymes, the moiety activities were decreased in fermentation supernatants. Parental XynA and Bs-Glu were superior to corresponding moieties in each fusion enzymes because of lower Kn higher kcat. Despite some variations, common optima were generally 50°C and pH 3.4 for the XynA moiety and parent, and 40°C and pH 6.4 for the Bs-Glu counterparts. Thus, the fusion enzyme XynA-Bs-Glu-1 and XynA-Bs-Glu-2 were bifunctional.

scholarly journals Expression, purification and characterization of a recombinant Tat47–57-Oct4 fusion protein in Pichia pastoris

2013 ◽  
Vol 9 (2) ◽  
pp. 471-475
Author(s):  
HAOTIAN WANG ◽  
XINMIN ZHANG ◽  
NING KONG ◽  
ANHUI WEI ◽  
YANHONG ZHANG ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Purification And Characterization

scholarly journals Biochemical and functional characterization of a recombinant monomeric factor VIII–Fc fusion protein

2013 ◽  
Vol 11 (1) ◽  
pp. 132-141 ◽  
Author(s):  
R. T. PETERS ◽  
G. TOBY ◽  
Q. LU ◽  
T. LIU ◽  
J. D. KULMAN ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Factor Viii ◽  
Functional Characterization ◽  
Fc Fusion Protein

Preparation and characterization of a novel exendin-4 human serum albumin fusion protein expressed in Pichia pastoris

2007 ◽  
Vol 14 (5) ◽  
pp. 588-595 ◽  
Author(s):  
Yan-Shan Huang ◽  
Zhi Chen ◽  
Yi-Qiong Chen ◽  
Guo-Chang MA ◽  
Jian-Feng Shan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Pichia Pastoris ◽  
Fusion Protein ◽  
Serum Albumin ◽  
Human Serum
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