Putative Folding Pathway of Insulin-like Growth Factor-I

Insulin-like growth factor-1 (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates. All of the intermediates have the disulfide bond between Cys18 and 61 formed, indicating...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1997-06, Vol.342 (2), p.298-305
Hauptverfasser:	Rosenfeld, Robert D., Miller, James A., Narhi, Linda O., Hawkins, Nessa, Katta, Viswanatham, Lauren, Scott, Weiss, Michael A., Arakawa, Tsutomu
Format:	Artikel
Sprache:	eng
Schlagworte:	Chromatography, High Pressure Liquid Copper Sulfate - pharmacology Disulfides - chemistry Disulfides - metabolism Glutathione - analogs & derivatives Glutathione - pharmacology Glutathione Disulfide Insulin-Like Growth Factor I - chemistry Insulin-Like Growth Factor I - metabolism Oxidation-Reduction Protein Folding Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - metabolism Trifluoroacetic Acid - pharmacology
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