Characterization of the three 125I-iodination isomers of human insulin-like growth factor I (IGF1)
- 8 December 1993
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1203 (2), 205-209
- https://doi.org/10.1016/0167-4838(93)90084-5
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- 1H-NMR Assignment and Secondary Structure of Human Insulin-Like Growth Factor-I(IGF-I) in SolutionThe Journal of Biochemistry, 1992
- Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I.CHEMICAL & PHARMACEUTICAL BULLETIN, 1992
- Development of an optimized refolding process for recombinant Ala–Glu–IGF-1Protein Engineering, Design and Selection, 1992
- Receptor binding and tyrosine kinase activation by insulin analogues with extreme affinities studied in human hepatoma HepG2 cellsDiabetes, 1991
- Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics studyBiochemistry, 1991
- Changing the insulin receptor to possess insulin-like growth factor I ligand specificityBiochemistry, 1990
- High-performance liquid chromatography of rat and mouse islet polypeptides: Potential risk of oxidation of methionine residues during sample preparationJournal of Chromatography B: Biomedical Sciences and Applications, 1990
- Monoiodoinsulin Labelled in Tyrosine Residue 16 or 26 of the B-Chain or 19 of the A-Chain. II. Characterization of the Kinetic Binding Constants and Determination of the Biological PotencyHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Biological potency and binding affinity of monoiodoinsulin with iodine in tyrosine A14 or tyrosine A19Biochemical and Biophysical Research Communications, 1979