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- Hober, SophiaKTH,Biokemi och biokemisk teknologi (author)
Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.
- Article/chapterEnglish1999
Publisher, publication year, extent ...
- 1999
- printrdacarrier
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- LIBRIS-ID:oai:DiVA.org:kth-184214
- https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-184214URI
- https://doi.org/10.1016/S0014-5793(98)01737-2DOI
- http://kipublications.ki.se/Default.aspx?queryparsed=id:1957251URI
Supplementary language notes
- Language:English
- Summary in:English
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Notes
- NR 20160331
- 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. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. 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.
Subject headings and genre
- NATURVETENSKAP Biologi hsv//swe
- NATURAL SCIENCES Biological Sciences hsv//eng
Added entries (persons, corporate bodies, meetings, titles ...)
- Lundström Ljung, J (author)
- Uhlén, MathiasKTH,Biokemi och biokemisk teknologi(Swepub:kth)u1dulvmw (author)
- Nilsson, B (author)
- KTHBiokemi och biokemisk teknologi (creator_code:org_t)
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- In:FEBS Letters443:30014-57931873-3468
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