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J. Biol. Chem., Vol. 261, Issue 6, 2489-2491, Feb, 1986
R Herrera, LM Petruzzelli and OM Rosen
Antipeptide antibodies directed to two amino acid sequences predicted from
the cDNA encoding the insulin proreceptor have been used to study the
relationship between the human receptors for insulin and insulin- like
growth factor I (IGF-I). An antibody directed to a cytoplasmic domain near
the membrane spanning region of the proreceptor inhibited the protein
tyrosine kinase activity of both receptors whereas an antibody directed to
the C terminus of the insulin receptor showed no cross-reactivity with the
IGF-I receptor. The results establish that the cloned cDNA from the human
placenta encodes the insulin receptor and not the closely related IGF-I
receptor, that the IGF-I and insulin receptors share a specific amino acid
sequence necessary for the expression of enzymatic activity, and that the C
terminus of the insulin receptor is not conserved in the IGF-I receptor.
Antibodies to deduced sequences of the insulin receptor distinguish conserved and nonconserved regions in the IGF-I receptor
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O. Rosen After insulin binds Science, September 18, 1987; 237(4821): 1452 - 1458. [Abstract] [PDF] |
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