Expression of Atypical and Classical Insulin Receptors in Chinese Hamster Ovary Cells Transfected with Cloned cDNA for the Human Insulin Receptor*

Endocrinology ◽  
1990 ◽  
Vol 127 (3) ◽  
pp. 1301-1309 ◽  
Author(s):  
HELEN A. JONAS ◽  
GLENN S. ECKARDT ◽  
STELLA CLARK
Endocrinology ◽  
1991 ◽  
Vol 129 (4) ◽  
pp. 2058-2066 ◽  
Author(s):  
YOSHIHIKO YAMAGUCHI ◽  
JEFFREY S. FLIER ◽  
ATSUSHI YOKOTA ◽  
HEIKE BENECKE ◽  
JONATHAN M. BACKER ◽  
...  

Biochemistry ◽  
1998 ◽  
Vol 37 (45) ◽  
pp. 15747-15757 ◽  
Author(s):  
Whaseon Lee-Kwon ◽  
Doekbae Park ◽  
Padmavathi V. Baskar ◽  
Sutapa Kole ◽  
Michel Bernier

1991 ◽  
Vol 6 (3) ◽  
pp. 231-239 ◽  
Author(s):  
P. McKinnon ◽  
M. Ross ◽  
J. R. E. Wells ◽  
F. J. Ballard ◽  
G. L. Francis

ABSTRACT Recombinant human insulin-like growth factor-I (hIGF-I) and a biologically potent variant lacking the N-terminal tripeptide (des(1–3)IGF-I) were produced from transfected Chinese hamster ovary cells. The constructs encoding the signal peptide, sequence of the mature peptide and a C-terminal extension peptide were expressed under the control of a Rous sarcoma virus promoter. Successfully transfected clones secreting correctly processed recombinant hIGF-I or des(1–3)IGF-I were selected by their secretion of IGF-I-like activity into the culture medium. The recombinant peptides were purified to homogeneity as assessed by high-performance liquid chromatography and N-terminal sequence analysis. The purified recombinant peptides exhibited biological potencies equivalent to authentic IGF-I and des(1–3)IGF-I respectively.


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