Characterization and Cloning of a Rat Insulin-Like Growth Factor Binding Protein

Autor:	Lorenzo Chiariotti, Yvonne W.-H. Yang, Joyce A. Romanus, Carmelo B. Bruni, Alexandra L. Brown, Craig C. Orlowski, Matthew M. Rechler
Rok vydání:	1989
Předmět:	Cloning biology Chemistry Binding protein Protein subunit DNA-binding protein Ligand blotting Insulin-like growth factor-binding protein medicine.anatomical_structure Biochemistry Extracellular medicine biology.protein Fibroblast
Zdroj:	Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors ISBN: 9781468456875
DOI:	10.1007/978-1-4684-5685-1_33
Popis:	The insulin-like growth factors, IGF-I and IGF-II, occur complexed to specific binding proteins in blood and other extracellular fluids.1 IGF-binding protein complexes of 150 kDa predominate in adult human and rat serum2,3, and also have been observed in human and porcine milk 4,5, and human fibroblast conditioned media6,7. Acid pH irreversibly dissociates the 150 kDa binding protein complex into an ~40 kDa acid-stable binding subunit.1 Recently, Baxter8 provided evidence for the existence of a second subunit of ~100 kDa that is unstable at acid pH and does not bind IGFs.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::54f5d7f057e8da36a3db9ebc165f5e6a https://doi.org/10.1007/978-1-4684-5685-1_33 Zobrazit plný text záznamu