scholarly journals Expression and characterization of recombinant human α-3/4-fucosyltransferase III from Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) cells using the baculovirus expression system

2001 ◽  
Vol 353 (3) ◽  
pp. 719 ◽  
Author(s):  
Vanessa A. MORAIS ◽  
Jacinta SERPA ◽  
Angelina S. PALMA ◽  
Teresa COSTA ◽  
Luis MARANGA ◽  
...  
Keyword(s):  
Spodoptera Frugiperda ◽  
Trichoplusia Ni ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Baculovirus Expression

Expression, Purification, and Characterization of Recombinant Human α1-Antitrypsin Produced Using Silkworm–Baculovirus Expression System

2018 ◽  
Vol 60 (12) ◽  
pp. 924-934 ◽  
Author(s):  
Yoshiki Morifuji ◽  
Jian Xu ◽  
Noriko Karasaki ◽  
Kazuhiro Iiyama ◽  
Daisuke Morokuma ◽  
...  
Keyword(s):  
Expression System ◽  
Baculovirus Expression System ◽  
Purification And Characterization ◽  
Baculovirus Expression

scholarly journals Partial characterization of natural and recombinant human soluble CD23

1992 ◽  
Vol 286 (3) ◽  
pp. 819-824 ◽  
Author(s):  
K Rose ◽  
G Turcatti ◽  
P Graber ◽  
S Pochon ◽  
P O Regamey ◽  
...  
Keyword(s):  
Insect Cells ◽  
Peptide Mapping ◽  
Sequence Similarity ◽  
Expression System ◽  
Protein A ◽  
Baculovirus Expression System ◽  
Partial Characterization ◽  
Disulphide Bonds ◽  
Baculovirus Expression

The purification to homogeneity of an active soluble 25 kDa fragment of CD23, produced in insect cells using the baculovirus expression system, is described. Peptide mapping and analysis by Edman degradation and mass spectrometry permitted partial characterization of the protein. A total of 165 out of 172 residues, including N-terminal and C-terminal regions, were mapped. The positions of the two disulphide bonds in the IgE-binding region were also determined: residue 110 is joined to residue 124, and residue 42 to residue 133. Natural CD23 25 kDa fragment was also analysed and found to possess the same disulphide bond arrangement. These results extend the previously noted sequence similarity with lectins to elements of secondary structure.

Purification and Characterization of Human Syk Produced Using a Baculovirus Expression System

2000 ◽  
Vol 18 (1) ◽  
pp. 86-94 ◽  
Author(s):  
Darren Baldock ◽  
Brent Graham ◽  
Mohammed Akhlaq ◽  
Patrick Graff ◽  
Carol E. Jones ◽  
...  
Keyword(s):  
Expression System ◽  
Baculovirus Expression System ◽  
Purification And Characterization ◽  
Baculovirus Expression
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