ISSN:
1573-4935
Keywords:
Somatomedins
;
insulin-like growth factors
;
purification
;
Mono-S
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
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 hIFG-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 competed less than 1% with hIGF-2 when the type 1 IGF receptor was blocked with insulin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01115047
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