scholarly journals Efficient production of recombinant PP2A at a low temperature using a baculovirus expression system

2016 ◽  
Vol 11 ◽  
pp. 86-89 ◽  
Author(s):  
Tsuyoshi Ikehara ◽  
Shihoko Nakashima ◽  
Junichi Nakashima ◽  
Tsubasa Kinoshita ◽  
Takeshi Yasumoto
Keyword(s):  
Low Temperature ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Efficient Production ◽  
Baculovirus Expression

scholarly journals High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization

1996 ◽  
Vol 319 (1) ◽  
pp. 191-195 ◽  
Author(s):  
Stuart A. ALI ◽  
Heidi C JOAO ◽  
Robert CSONGA ◽  
Franz HAMMERSCHMID ◽  
Alexander STEINKASSERER
Keyword(s):  
Human Serum ◽  
Expression System ◽  
Baculovirus Expression System ◽  
High Yield ◽  
Efficient Production ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
Mammalian Expression ◽  
Baculovirus Expression ◽  
Wide Range

Recently, there has been much interest in expressing recombinant human serum transferrin (HST) and mutants thereof for structural and functional studies. We have developed a baculovirus expression system for the rapid and efficient production of large quantities of HST (> 20 mg/l). Like native HST, the recombinant protein can bind two ferric ions in the presence of bicarbonate, and is actively taken up by receptor-mediated endocytosis. Secondary structure calculations from CD measurements indicate a content of 42% α-helix and 28% β-sheet. This is the first reported use of a non-mammalian expression system to produce functional HST, and will provide a practical tool to allow expression of a wide range of HST variants for mutagenesis studies.

scholarly journals Expression of functional G protein beta gamma dimers of defined subunit composition using a baculovirus expression system.

1992 ◽  
Vol 267 (19) ◽  
pp. 13123-13126 ◽  
Author(s):  
S.G. Graber ◽  
R.A. Figler ◽  
V.K. Kalman-Maltese ◽  
J.D. Robishaw ◽  
J.C. Garrison
Keyword(s):  
G Protein ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Subunit Composition ◽  
Baculovirus Expression

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.

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