Differential stability of recombinant human insulin-like growth factor II in Escherichia coli and Staphylococcus aureus

1990 ◽  
Vol 14 (3-4) ◽  
pp. 423-437 ◽  
Author(s):  
Björn Hammarberg ◽  
Tomas Moks ◽  
Michael Tally ◽  
Anette Elmblad ◽  
Erik Holmgren ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Growth Factor ◽  
Human Insulin ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Factor Ii ◽  
Differential Stability ◽  
And Staphylococcus Aureus

Recombinant Human Insulin-Like Growth Factor II Expressed in Escherichia coli

1987 ◽  
Vol 5 (10) ◽  
pp. 1047-1051 ◽  
Author(s):  
Thomas C. Furman ◽  
Janet Epp ◽  
Hansen M. Hsiung ◽  
JoAnn Hoskins ◽  
George L. Long ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Growth Factor ◽  
Human Insulin ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Factor Ii

Expression of secreted recombinant human insulin-like growth factor-II (IGF-II) in Chinese hamster ovary cells

1994 ◽  
Vol 36 (1) ◽  
pp. 75-83
Author(s):  
Hicham Bekkari ◽  
Driss Sekkat ◽  
Jean Straczek ◽  
Ketsia Hess ◽  
Francine Belleville-Nabet ◽  
...  
Keyword(s):  
Growth Factor ◽  
Human Insulin ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Ovary Cells ◽  
Factor Ii

scholarly journals Dual affinity fusion approach and its use to express recombinant human insulin-like growth factor II.

1989 ◽  
Vol 86 (12) ◽  
pp. 4367-4371 ◽  
Author(s):  
B. Hammarberg ◽  
P. A. Nygren ◽  
E. Holmgren ◽  
A. Elmblad ◽  
M. Tally ◽  
...  
Keyword(s):  
Growth Factor ◽  
Human Insulin ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Factor Ii ◽  
Fusion Approach

scholarly journals Separation and characterization of modified variants of recombinant human insulin-like growth factor I derived from a fusion protein secreted from Escherichia coli

1990 ◽  
Vol 271 (2) ◽  
pp. 357-363 ◽  
Author(s):  
G Forsberg ◽  
G Palm ◽  
A Ekebacke ◽  
S Josephson ◽  
M Hartmanis
Keyword(s):  
Escherichia Coli ◽  
Growth Factor ◽  
Fusion Protein ◽  
Human Insulin ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Factor I ◽  
Methionine Residue ◽  
Igf I ◽  
Growth Factor I

Human insulin-like growth factor I, IGF-I, was produced in Escherichia coli fused to a synthetic IgG-binding peptide The fusion protein is secreted into the medium during fermentation and was initially purified on an IgG-Sepharose column. After hydroxylamine cleavage, IGF-I was purified to homogeneity. During purification, impurities in the form of modified variants of IGF-I were detected and characterized. The closely related impurities were identified to be a misfolded form of IGF-I, having mismatched disulphide bonds, a form with the single methionine residue in IGF-I oxidized to methionine sulphoxide and a variant in which the methionine residue was substituted by a norleucine residue during protein synthesis. A form proteolytically cleaved between two arginine residue was also detected. These impurities were separated from the major component, native IGF-I, by using reverse-phase h.p.l.c. The modified molecules as well as native IGF-I were characterized both as intact molecules and as fragments, after pepsin digestion, using the techniques of plasma desorption m.s., N-terminal sequencing and amino acid analysis. The oxidized form was 90%, and the norleucine analogue was 70%, as potent as native IGF-I in a biological radioreceptor assay, and the form having mismatched disulphides lacked receptor affinity.

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