Monoiodoinsulin Labelled in Tyrosine Residue 16 or 26 of the Insulin B-Chain. Preparation and Characterization of some Binding Properties
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (1), 573-580
- https://doi.org/10.1515/bchm2.1981.362.1.573
Abstract
By the combination of polyacrylamide gel electrophoresis and QAE-Sephadex ion exchange chromatography it was possible to isolate the 4 isomers of porcine [125I]monoiodoinsulin to a purity of more than 97%. The yield of the 2 B-chain-labeled isomers was increased by iodinating in buffer containing 6 M urea. The apparent binding affinity to isolated rat adipocytes was 0.65 for the A19 isomer, 1.0 for the B16 isomer and 2.0 for the B26 isomer, respectively, relative to the A14 isomer. The B26 isomer had only an apparent binding affinity of 1.2 relative to the A14 isomer in isolated hepatocytes.This publication has 17 references indexed in Scilit:
- MONOIODOINSULIN SPECIFICALLY SUBSTITUTED IN TYR A14 OR TYR A19International Journal of Peptide and Protein Research, 1980
- Biological potency and binding affinity of monoiodoinsulin with iodine in tyrosine A14 or tyrosine A19Biochemical and Biophysical Research Communications, 1979
- The viability of cells grown or centrifuged in a new density gradient medium, Percoll(TM)Experimental Cell Research, 1977
- Cooperativity in ligand binding: A new graphic analysisBiochemical and Biophysical Research Communications, 1975
- PREPARATION AND CHARACTERIZATION OF MONOIODOINSULINInternational Journal of Peptide and Protein Research, 1974
- MonoiodoinsulinPublished by Elsevier ,1974
- HIGH-YIELD PREPARATION OF ISOLATED RAT LIVER PARENCHYMAL CELLSThe Journal of cell biology, 1969
- The reactivity of the tyrosine residues in insulin with respect to iodine IIRecueil des Travaux Chimiques des Pays-Bas, 1961