Journal
PEPTIDES
Volume 24, Issue 6, Pages 863-872Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0196-9781(03)00166-9
Keywords
amphibian; peptides; cloning; kininogen; molecular evolution
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Bradykinin, (des-Arg(9))-bradykinin and bradykinyl-VAPAS, were identified in the skin secretion of the piebald odorous frog, Odorrana schmackeri. Using 3'- and 5'-RACE reactions, bradykinin precursor cDNA was cloned and found to contain an open-reading frame of 311 amino acid residues. The preprobradykinin was found to consist of a putative signal peptide of approximately 20 amino acid residues, followed by seven tandem repeat coding domains of 43-44 amino acids. Bradykinin and its C-terminal extended molecular form were encoded on this single precursor and could be generated by differential post-translational processing. (C) 2003 Elsevier Inc. All rights reserved.
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