Title : Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.

Pub. Date : 1999 Jan 29

PMID : 10025946






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. Disulfides insulin like growth factor 1 Homo sapiens
2 Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. Disulfides insulin like growth factor 1 Homo sapiens
3 The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Disulfides insulin like growth factor 1 Homo sapiens
4 Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance. Disulfides insulin like growth factor 1 Homo sapiens
5 Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance. Disulfides insulin like growth factor 1 Homo sapiens