Analysis of the Human Insulin Receptor
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 915-924
- https://doi.org/10.1515/bchm3.1992.373.2.915
Abstract
The insulin derivative 4-azidosalicyloyl-[B1-biocytin-B2-lysine]insulin was used to photo-affinity-label the highly purified insulin receptor from human placenta. As shown by SDS-polyacrylamide gel electrophoresis, the 5 monoiodo isomers, with iodine in positions B1, B16, B26, A14 or A19, gave different labelling patterns. After complete tryptic digestion of the covalent receptor complex with 125I-Asa-[BctB1,LysB2]insulin, a stable fragment of 18 kDa was isolated, which was further purified by HPLC. This tryptic fragment of the intact receptor corresponds, according to HPLC, Tricin-SDS-PAGE and 2D-electrophoresis, to the similarly labelled sequenced domain of the receptor ectodomain (Fabry, M. et al. (1992) J. Biol. Chem. 267, 8950-8956). We thus conclude that insulin is bound to identical contact sites of native receptor and truncated ectodomain.Keywords
This publication has 8 references indexed in Scilit:
- The insulin‐binding domain of insulin receptor is encoded by exon 2 and exon 3Journal of Cellular Biochemistry, 1992
- Design and Synthesis of a Novel Biotinylated Photoreactive Insulin for Receptor AnalysisBiological Chemistry Hoppe-Seyler, 1992
- The ligand specificities of the insulin receptor and the insulin-like growth factor I receptor reside in different regions of a common binding site.Proceedings of the National Academy of Sciences, 1991
- Functional labeling of insulin receptor subunits in live cellsPublished by Elsevier ,1989
- Intrinsic Kinase Activity of the Insulin ReceptorPublished by Elsevier ,1989
- Differential sensitivity of two functions of the insulin receptor to the associated proteolysis: kinase action and hormone binding.Proceedings of the National Academy of Sciences, 1986
- Internalization and molecular processing of insulin receptors in isolated rat adipocytes.Proceedings of the National Academy of Sciences, 1982
- Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries.Proceedings of the National Academy of Sciences, 1980