Three ichthyotoxic peptides, pardaxins P-I to P-3, have been isolated from the defense secretion of the sole Pardachirus pavoninus. Pavoninins, the steroid glycosides with shark-repelling ability, had previously been isolated therefrom. Each pardaxin consists of 33 amino acid residues having a distinctly hydrophilic carboxyl terminal region and a predominantly hydrophobic remainder; the pardaxin is thus strongly surfactant. These peptides show marked physical and pharmacological similarities to melittin, the major active constituent of bee venom, yet they lack sequence homology. They are probably also responsible for the predator-repelling property of the sole.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
Three ichthyotoxic peptides, pardaxins P-I to P-3, have been isolated from the defense secretion of the sole Pardachirus pavoninus. Pavoninins, the steroid glycosides with shark-repelling ability, had previously been isolated therefrom. Each pardaxin consists of 33 amino acid residues having a distinctly hydrophilic carboxyl terminal region and a predominantly hydrophobic remainder; the pardaxin is thus strongly surfactant. These peptides show marked physical and pharmacological similarities to melittin, the major active constituent of bee venom, yet they lack sequence homology. They are probably also responsible for the predator-repelling property of the sole.
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| skos:exactMatch | |
| uniprot:name |
Science
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| uniprot:author |
Kubota I.,
Nakanishi K.,
Tachibana K.,
Thompson S.A.
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| uniprot:date |
1986
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| uniprot:pages |
341-343
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| uniprot:title |
Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus.
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| uniprot:volume |
233
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| dc-term:identifier |
doi:10.1126/science.233.4761.341
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