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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
A bradykinin-potentiating peptide (peptide K
12
) isolated from the venom of Egyptian scorpion Buthus occitanus
Peptides, Volume 16, No. 8, Year 1995
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Description
A nontoxic peptide with bradykinin-potentiating activity was isolated from the dialyzed venom of the scorpion Buthus occitanus by reverse-phase high performance liquid chromatography (RP-HPLC). The pharmacological activity of the peptide was bioassayed by its ability to potentiate added bradykinin (BK) on the isolated guinea pig ileum as well as the isolated rat uterus for contraction. Moreover, the peptide potentiates in vivo the depressor effect of BK on arterial blood pressure in the normotensive anesthetized rat. Chemical characterization of the peptide was also performed. The amino acid composition of the peptide showed 21 amino acid residues per molecule including three proline residues. The amino acid sequence of the purified peptide was confirmed by mass spectrometry. Either N- or C-terminal ends were free. The sequence does not show a homology with bradykinin-potentiating peptides isolated from either scorpion or snake venoms. Furthermore, we did not find a significant sequence homology between the sequence of the isolated peptide and any of proteins or peptides in GenPro or NBRF data banks. The peptide also inhibited angiotensin-converting enzyme (ACE), and could not serve as substrate for the enzyme. It could be concluded that the mechanism of bradykinin-potentiating peptide (BPP) activity may be due to ACE inhibition. © 1995.
Authors & Co-Authors
Meki, Abdel Raheim M.A.
Egypt, Asyut
Assiut University
Nassar, Ahmed Yassein A.
Egypt, Asyut
Assiut University
Rochat, Hervè
France, Marseille
Aix Marseille Université
Statistics
Citations: 81
Authors: 3
Affiliations: 2
Identifiers
Doi:
10.1016/0196-9781(95)02036-5
ISSN:
01969781
Research Areas
Noncommunicable Diseases
Study Locations
Guinea