http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11304
A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion (Articolo in rivista)
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- Label
- A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Alternative label
Miele R, Borro M, Mangoni ML, Simmaco M, Barra D. (2003)
A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion
in Peptides (New York, NY : 1980)
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- Miele R, Borro M, Mangoni ML, Simmaco M, Barra D. (literal)
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- D. Barra รจ a disposizione dell'IBPM (literal)
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- ISI Web of Science (WOS) (literal)
- Titolo
- A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion (literal)
- Abstract
- In amphibian skin secretions, a peptidylprolyl cis/trans isomerase activity was detected. A Xenopus laevis skin cDNA coding for this protein was cloned, sequenced and over-expressed in Escherichia coli. The primary structure of the protein shows extensive similarity with members of
the cyclophilin A family. Catalytic parameters of the recombinant protein are similar to those of the human enzyme. The enzymatic activity is inhibited by cyclosporin A. Data suggesting that peptidylprolyl isomerization influences the biological activity of antibacterial peptides of amphibian origin are presented, and its putative role in the defence mechanism discussed. (literal)
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