Expression and Purification of Biologically Active Rat Bone Morphogenetic Protein-4 produced as Inclusion Bodies in Recombinant Escherichia coli

2005 ◽  
Vol 27 (20) ◽  
pp. 1559-1564 ◽  
Author(s):  
Burkhard Klösch ◽  
Walter Fürst ◽  
Rudolf Kneidinger ◽  
Monika Schuller ◽  
Barbara Rupp ◽  
...  
2018 ◽  
Vol 18 ◽  
pp. e00249
Author(s):  
Gesa-Maria Gieseler ◽  
Kimia Ekramzadeh ◽  
Volker Nölle ◽  
Svitlana Malysheva ◽  
Henning Kempf ◽  
...  

1999 ◽  
Vol 64 (8) ◽  
pp. 1348-1356 ◽  
Author(s):  
Michaela Rumlová-Kliková ◽  
Iva Pichová ◽  
Eric Hunter ◽  
Tomáš Ruml

It has been generally accepted that inclusion bodies (IBs) formed in Escherichia coli consist of non-biologically active aggregated proteins, which are stabilized by non-productive interactions. We show here that bacterial expression of a retroviral capsid polyprotein results in formation of insoluble IBs that contain fully assembled viral particles connected with amorphous material. The efficiency of IBs formation and capsid assembly was not significantly affected by changes in induction temperature, pH of cultivation medium or the level of expression.


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