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Purification and Micro Sequence Analysis of Active Peptides from Amphibian Skins

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Methods in Protein Sequence Analysis

Part of the book series: Experimental Biology and Medicine ((EBAM,volume 3))

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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.).

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© 1982 The HUMANA Press Inc.

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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

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  • 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

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