ISOLATION AND AMINO ACID COMPOSITION OF SAUVAGINE

Authors:
Publisher website
Google Scholar
Abstract
The skin of the South American frog Phyllomedusa sauvagei contains a new active polypeptide, sauvagine, which does not belong to any of the peptide families hitherto described in the amphibian skin. Sauvagine was isolated in a pure form starting from crude methanol extracts. The purification procedure involved several successive steps: dialysis, precipitation with ethanol and acetone, gel filtration and ion exchange chromatography. Two forms of sauvagine were separated. The major component (sauvagine I) was submitted to acid hydrolysis. The sauvagine molecule appeared to possess clear hydrophobic characteristics and to consist of a straight chain of 40 amino acid residues, among which the glutamyl‐, aspartyl‐ leucyl‐ and isoleucyl‐residues were particularly well represented. The elucidation of the amino acid sequence in the sauvagine molecule is in progress.

This publication has 18 references indexed in Scilit: