Article
Deletion of residues 485-599 from the human insulin receptor abolishes antireceptor antibody binding and influences tyrosine kinase activation.
Molecular endocrinology (Baltimore, Md.) - 1 Mar 1994
Sung C K, Wong K Y, Yip C C, Hawley D M, Goldfine I D
Abstract excerpt
We have studied insulin and antireceptor antibody binding to mutated human insulin receptors deleted of residues 485-599 in the alpha-subunit by site-directed mutagenesis. Both normal and mutated receptors were expressed in rat HTC hepatoma cells. Cells expressing either the normal receptor or the mutated receptor retained the ability to bind insulin. In contrast to the normal receptor, however, the mutated...
Topics
- Animals
- Antibodies, Monoclonal
- Base Sequence
- Blotting, Western
- DNA, Neoplasm
- Enzyme Activation
- Gene Deletion
- Humans
- Insulin
- Iodine Radioisotopes
- Liver Neoplasms, Experimental