Open AccesscDNA cloning of bradykinin‐potentiating peptides–C‐type natriuretic peptide precursor, and characterization of the novel peptide Leu3‐blomhotin from the venom of Agkistrodon blomhoffi
Author(s) -
Murayama Nobuhiro,
Michel Gilles H.,
Yanoshita Ryohei,
Samejima Yuji,
Saguchi Kenichi,
Ohi Hiroaki,
Fujita Yoshiaki,
Higuchi Shigesada
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01443.x
Subject(s) - peptide sequence , venom , complementary dna , bradykinin , peptide , cdna library , microbiology and biotechnology , signal peptide , biology , cardiotoxin , biochemistry , chemistry , receptor , gene
A cDNA clone, 1.8 kb long, was isolated from a venom gland cDNA library of Agkistrodon blomhoffi that encodes a large plurifunctional precursor composed of 263 amino‐acid residues. Nucleotide sequence analysis of this clone revealed that sequences which code for blomhotin and a novel peptide Leu3‐blomhotin are located in the N‐terminal region of the precursor polypeptide, followed by four tandemly aligned sequences which code for three types of bradykinin‐potentiating peptide. In the C‐terminal region, the sequence for the C‐type natriuretic peptide was located along with a preceding processing signal. The deduced amino‐acid sequences for the four bradykinin‐potentiating peptides coincided exactly with previously known sequences for potentiator B, potentiator C and potentiator E. The actual Leu3‐blomhotin peptide was subsequently isolated from the venom of A. blomhoffi and characterized. Leu3‐blomhotin possesses contractile activity in isolated rat stomach fundus smooth muscle in the same manner as blomhotin. Furthermore, it was shown that blomhotin and Leu3‐blomhotin retained activity to inhibit the angiotensin‐converting enzyme.