scholarly journals Glycoforms obtained by expression in Pichia pastoris improve cancer targeting potential of a recombinant antibody-enzyme fusion protein

Glycobiology ◽  
2003 ◽  
Vol 14 (1) ◽  
pp. 27-37 ◽  
Author(s):  
K. F. Medzihradszky
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Recombinant Antibody ◽  
Cancer Targeting ◽  
Enzyme Fusion

scholarly journals Recombinant production of a peroxidase-protein G fusion protein in Pichia pastoris

2016 ◽  
Vol 219 ◽  
pp. 24-27 ◽  
Author(s):  
Florian Wolfgang Krainer ◽  
Barbara Darnhofer ◽  
Ruth Birner-Gruenberger ◽  
Anton Glieder
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Protein G ◽  
Recombinant Production

Atypical Processing of Amyloid Precursor Fusion Protein by Proteolytic Activity in Pichia pastoris,

1999 ◽  
Vol 263 (2) ◽  
pp. 596
Author(s):  
Adam Markaryan ◽  
Irina Morozova ◽  
Bao-Shiang Lee ◽  
Arnold Kaplan
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Proteolytic Activity

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.

High-level expression, purification and study of bioactivity of fusion protein M-IL-2(88Arg, 125Ala) in Pichia pastoris

2014 ◽  
Vol 101 ◽  
pp. 99-105 ◽  
Author(s):  
Lin Li ◽  
Dongmeng Qian ◽  
Guangcan Shao ◽  
Zhiyong Yan ◽  
Ronggui Li ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
High Level Expression ◽  
High Level

Immunoenzymometric Assay for a Small Molecule,11-Deoxycortisol, with Attomole-Range Sensitivity Employing an scFv−Enzyme Fusion Protein and Anti-Idiotype Antibodies

2006 ◽  
Vol 78 (7) ◽  
pp. 2244-2253 ◽  
Author(s):  
Norihiro Kobayashi ◽  
Keiichi Iwakami ◽  
Shuhei Kotoshiba ◽  
Toshifumi Niwa ◽  
Yoshinori Kato ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Small Molecule ◽  
Enzyme Fusion
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