title: An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process.
abstract: The separation of human insulin-like growth factors hIGF-1 and hIGF-2 was greatly improved by an additional purification step using the cation exchanger Mono-S (FPLC) compared to previous studies. Cross-reactions between hIGF-1 and hIGF-2 were strongly reduced. The more highly purified hIGF-1 had a cross-reaction of less than 1% in the RIA for hIGF-2, and was equivalent to recombinant hIGF-1. The pure hIGF-2 had a cross-reaction of less than 1% in the RIA for hIGF-1. In the human placental hIGF-2 radioreceptor assay, the hIGF-1 polypeptide completed less than 1% with hIGF-2 when the type 1 IGF receptor was blocked with insulin.
authors.affiliation: Department of Endocrinology, Karolinska Institutet, Stockholm, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Tally
authors.forename: K
authors.initials: K
authors.lastname: Florell
authors.forename: G
authors.initials: G
authors.lastname: Enberg
mesh_terms: D002411:Cation Exchange Resins; D002852:Chromatography, Ion Exchange / Q000379:methods; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000097:blood / Q000302:isolation & purification*; D007335:Insulin-Like Growth Factor II / Q000097:blood / Q000302:isolation & purification*; D008722:Methods; D011863:Radioimmunoassay; D013002:Somatomedins / Q000302:isolation & purification*
chemical_list: D002411:Cation Exchange Resins; D013002:Somatomedins; D007334:Insulin-Like Growth Factor I; D007335:Insulin-Like Growth Factor II