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dc.contributor.authorProaño Bolaños, Carolina-
dc.contributor.authorLi, Renjie-
dc.contributor.authorZhou, Mei-
dc.contributor.authorWang, Lei-
dc.contributor.authorXi, Xinping-
dc.contributor.authorTapia, Elicio E.-
dc.contributor.authorColoma, Luis A.-
dc.contributor.authorChen, Tianbao-
dc.contributor.authorShaw, Chris-
dc.identifier.citationProaño Bolaños, C., Li, R., Zhou, M., Wang, L., Xi, X., Tapia, E. E., … Shaw, C. (2017). Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer. EuPA Open Proteomics, 15, 1–13. doi:10.1016/j.euprot.2017.02.001es
dc.description.abstractPeptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X(7)-C-X(6,7)-C-X(6,7)-Y-X(3)-C-X(2)-C-X(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.es
dc.relation.ispartofseriesPRODUCCIÓN CIENTÍFICA-ARTÍCULOS;A-IKIAM-000071-
dc.subjectKazal-type proteinase inhibitorses
dc.subjectFrog skin secretiones
dc.subjectMolecular cloning-
dc.subjectTandem mass spectrometry-
dc.subjectCruziohyla calcarifer-
dc.titleNovel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcariferes
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