Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide
Article first published online: 21 NOV 2012
© 2012 The Authors Journal compilation © 2012 FEBS
Volume 279, Issue 24, pages 4589–4597, December 2012
How to Cite
Landreh, M., Alvelius, G., Willander, H., Stukenborg, J.-B., Söder, O., Johansson, J. and Jörnvall, H. (2012), Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide. FEBS Journal, 279: 4589–4597. doi: 10.1111/febs.12045
- Issue published online: 4 DEC 2012
- Article first published online: 21 NOV 2012
- Accepted manuscript online: 26 OCT 2012 12:00AM EST
- Manuscript Revised: 22 OCT 2012
- Manuscript Accepted: 22 OCT 2012
- Manuscript Received: 8 SEP 2012
Fig. S1. ESI-MS spectra of insulin, C-peptide and insulin + C-peptide at pH 5, HCl, pH 4, acetic acid, and pH 5–8 in ammonium acetate.
Fig. S2. A500 of insulin, C-peptide and insulin + C-peptide in acetic acid, pH 4, and ammonium acetate, pH 5–8.
Fig. S3. Electron microscopy of insulin (top panel), C-peptide (middle panel) and the insulin–C-peptide precipitate (lower panel).
Fig. S4. A280 of 100 μL of a 100 μm insulin standard (blue) and 100 μL each of the pellet (red) and supernatant (green) fractions.
Fig. S5. Chemically inducible dimerization of heteromers between insulin and E3,11,27A C-peptide.
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