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Abstract:
We have isolated a novel bradykinin B-2-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/Ile-Arg.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. (C) 2003 Elsevier B.V. All rights reserved.
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REGULATORY PEPTIDES
ISSN: 0167-0115
Year: 2003
Issue: 1-3
Volume: 116
Page: 147-154
2 . 2 3 5
JCR@2003
1 . 8 1 3
JCR@2015
JCR Journal Grade:2
Cited Count:
WoS CC Cited Count: 20
SCOPUS Cited Count: 21
ESI Highly Cited Papers on the List: 0 Unfold All
WanFang Cited Count:
Chinese Cited Count:
30 Days PV: 1
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