Abstract
PEPTIDE PURIFICATION. In addition to the normally routine methods, we have applied the following techniques to solve some structural problems observed during the isolation of active peptides from amphibian skins: (i) isoelectric focusing in combination with electrophoresis to separate sauvagine I and II; (ii) reverse-phase HPLC to purify dermorphins and triptokinins; in particular, HPLC appears to be a versatile technique to isolate isocratically (on a / Bondapak C-18 column) caerulein from the analogue beta Asp3-caerulein (using as eluent 30% MeOH-10% MeCN in 0.02 M NH4OAc at pH 3.5), probably because of a different protonation of their aspartyl residues at the 3rd position; these results are in accordance with those obtained on HVPE at pH 2.7 (pyridine/glacial acetic acid/water 1/100/899 by vol.).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 The HUMANA Press Inc.
About this chapter
Cite this chapter
Montecucchi, P.C., Gozzini, L. (1982). Purification and Micro Sequence Analysis of Active Peptides from Amphibian Skins. In: Elzinga, M. (eds) Methods in Protein Sequence Analysis. Experimental Biology and Medicine, vol 3. Humana Press. https://doi.org/10.1007/978-1-4612-5832-2_64
Download citation
DOI: https://doi.org/10.1007/978-1-4612-5832-2_64
Publisher Name: Humana Press
Print ISBN: 978-1-4612-5834-6
Online ISBN: 978-1-4612-5832-2
eBook Packages: Springer Book Archive