Article
The ligand binding characteristics of a kinase-defective A/K1018 human insulin receptor expressed in Rat 1 fibroblasts.
Biochimica et biophysica acta - 12 Jul 1990
Maegawa H, Kobayashi M, Egawa K, McClain D A, Olefsky J M, Shigeta Y
Abstract excerpt
Expression of the cDNA encoding a human insulin receptor with replacement of alanine for lysine at residue 1018 in the ATP binding domain of the beta subunit results in a receptor that is not only kinase-defective, but also biologically inactive. Interestingly, this mutated receptor shows a decreased insulin binding affinity when expressed at high level. We, therefore, studied the binding property of this mutant...
Topics
- Animals
- Cell Line
- Fibroblasts
- Humans
- Hydrogen-Ion Concentration
- Insulin
- Kinetics
- Ligands
- Mutation
- Protein Kinases
- Rats
- Receptor, Insulin