scholarly journals Characterization of Feline CD56 Molecule Expressed on Insect Cells by the Baculovirus Expression System

1999 ◽  
Vol 61 (6) ◽  
pp. 701-703 ◽  
Author(s):  
Yorihiro NISHIMURA ◽  
Takayuki MIYAZAWA ◽  
Yasuhiro IKEDA ◽  
Yoshihiro IZUMIYA ◽  
Kazuya NAKAMURA ◽  
...  
Keyword(s):  
Insect Cells ◽  
Expression System ◽  
Baculovirus Expression System ◽  
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.

scholarly journals Production, processing and partial purification of functional G protein βγ subunits in baculovirus-infected insect cells

1992 ◽  
Vol 286 (3) ◽  
pp. 677-680 ◽  
Author(s):  
J D Robishaw ◽  
V K Kalman ◽  
K L Proulx
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Insect Cells ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Partial Purification ◽  
Baculovirus Expression ◽  
Gamma Subunits ◽  
Infected Insect ◽  
Beta 2

As a result of the inability to resolve the heterogeneous mixture of G protein beta gamma subunits present in tissues, it has not been possible to compare different beta gamma subunits of the G proteins in terms of their proposed roles in receptor-effector coupling. This study was undertaken to establish the utility of the baculovirus expression system in producing homogeneous beta gamma subunits of defined composition for the comparative analysis of these subunits in reconstitution systems. In this study we report the expression, and appropriate post-translational processing, of recombinant beta 2, gamma 2 and gamma 3 subunits. In addition, we show that the recombinant beta gamma subunits can be readily purified, and can functionally interact with the alpha subunits of the G proteins.

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
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