Air-lift Bioreactor Improvement of Scale-up Linearity Between Shake Flasks and 25-L Scale in the Insect Cells—baculovirus Expression System

2007 ◽  
pp. 807-809
Author(s):  
Frédéric Bollin ◽  
Christophe Losberger ◽  
Laurent Chevalet ◽  
Thierry Battle
Keyword(s):  
Insect Cells ◽  
Expression System ◽  
Scale Up ◽  
Baculovirus Expression System ◽  
Baculovirus Expression ◽  
Shake Flasks ◽  
Air Lift

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.

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.

Strong buffering capacity of insect cells. Implications for the baculovirus expression system

1995 ◽  
Vol 17 (1) ◽  
pp. 21-26 ◽  
Author(s):  
Miguel Medina ◽  
Abelardo L�pez-Rivas ◽  
Douwe Zuidema ◽  
Graham J. Belsham ◽  
Esteban Domingo ◽  
...  
Keyword(s):  
Insect Cells ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Buffering Capacity ◽  
Baculovirus Expression

scholarly journals Synthesis of tetanus toxin fragment C in insect cells by use of a baculovirus expression system.

1991 ◽  
Vol 59 (5) ◽  
pp. 1627-1632 ◽  
Author(s):  
I G Charles ◽  
B C Rodgers ◽  
A J Makoff ◽  
S N Chatfield ◽  
D E Slater ◽  
...  
Keyword(s):  
Tetanus Toxin ◽  
Insect Cells ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Baculovirus Expression
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