Construction, Purification, and Characterization of a Homodimeric Granulocyte Colony-Stimulating Factor

2017 ◽  
Vol 59 (9-10) ◽  
pp. 374-384 ◽  
Author(s):  
Gitana Mickiene ◽  
Indre Dalgediene ◽  
Zilvinas Dapkunas ◽  
Gintautas Zvirblis ◽  
Henrikas Pesliakas ◽  
...  
Keyword(s):  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Purification And Characterization ◽  
Stimulating Factor

scholarly journals Purification and characterization of human granulocyte colony-stimulating factor (G-CSF).

1986 ◽  
Vol 5 (5) ◽  
pp. 871-876 ◽  
Author(s):  
H. Nomura ◽  
I. Imazeki ◽  
M. Oheda ◽  
N. Kubota ◽  
M. Tamura ◽  
...  
Keyword(s):  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Purification And Characterization ◽  
Stimulating Factor ◽  
Factor G

Purification and characterization of two recombinant human granulocyte colony-stimulating factor glycoforms

1999 ◽  
Vol 11 (2) ◽  
pp. 117-128 ◽  
Author(s):  
Luigi Rotondaro ◽  
Enrico De Paolis ◽  
Dario Ferrero ◽  
Laura D’Alatri ◽  
Giuseppe Raucci ◽  
...  
Keyword(s):  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Purification And Characterization ◽  
Stimulating Factor

scholarly journals Characterization of recombinant-derived granulocyte-colony stimulating factor (G-CSF)

1988 ◽  
Vol 256 (1) ◽  
pp. 213-218 ◽  
Author(s):  
P Wingfield ◽  
R Benedict ◽  
G Turcatti ◽  
B Allet ◽  
J J Mermod ◽  
...  
Keyword(s):  
Coli Strain ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Wild Type ◽  
Disulphide Bonds ◽  
Disulphide Bond Formation ◽  
Stimulating Factor ◽  
Factor G

Human granulocyte colony-stimulating factor (G-CSF), and a mutant having a Ser for Cys substitution at residue 18 were produced in Escherichia coli strain W3110. About 60 mg of pure protein was obtained from 50 g of wet cells with a recovery of about 20%. The proteins were characterized physically and chemically, including determination of disulphide bonds, which were found to exist between residues 37-43 and 65-75. Cys-18 is not involved in disulphide bond formation and was substituted by Ser with no effects on gross protein conformation or biological activity. Both the wild-type and the mutant recombinant-derived proteins, although not glycosylated, possess colony-stimulating activities. In a bioassay using the murine myelomonocytic leukaemic cell line WEH1 3B D+, activities were obtained which were similar to those of natural G-CSF and of a glycosylated recombinant-derived human G-CSF produced in monkey cells.

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