Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima
| Autor: | Pingfan Rao, Tianbao Chen, Martin O'Rourke, David F. Orr, David G. Hirst, Christopher Shaw, Daniel J.M. Coulter |
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| Rok vydání: | 2003 |
| Předmět: |
Male
DNA Complementary Receptor Bradykinin B2 Physiology Molecular Sequence Data Clinical Biochemistry Bradykinin Peptide Toad Bombina maxima Biochemistry Phenylephrine Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Salientia biology.animal Bradykinin B2 Receptor Antagonists Animals Amino Acid Sequence Rats Wistar Skin chemistry.chemical_classification Base Sequence integumentary system Molecular mass biology cDNA library biology.organism_classification Rats Vasodilation chemistry Anura Peptides B2 Bradykinin Receptor Sequence Alignment |
| Zdroj: | Regulatory Peptides. 116:147-154 |
| ISSN: | 0167-0115 |
| DOI: | 10.1016/j.regpep.2003.08.003 |
| Popis: | We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/IleArg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin. D 2003 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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