Chen Tianbao, O'Rourke Martin, Orr David F, Coulter Daniel J M, Hirst David G, Rao Pingfan, Shaw Chris
School of Biomedical Sciences, University of Ulster, Coleraine BT52 1SA, Northern Ireland, UK.
Regul Pept. 2003 Nov 15;116(1-3):147-54. doi: 10.1016/j.regpep.2003.08.003.
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.
我们从大蹼铃蟾（Bombina maxima）的防御性皮肤分泌物中分离出一种新型缓激肽B(2)受体拮抗剂肽——激肽抑制素。质谱分析确定其分子量为931.56 Da，并得出一个暂定结构：焦谷氨酸-亮氨酸/异亮氨酸-脯氨酸-甘氨酸-亮氨酸/异亮氨酸-甘氨酸-脯氨酸-亮氨酸/异亮氨酸-精氨酸-酰胺。在对已测序的大蹼铃蟾皮肤cDNA文库数据库进行查询后发现，未修饰序列-QIPGLGPLRG-位于一个116个氨基酸残基的开放阅读框的C末端。这证实了成熟肽上存在的翻译后修饰具有适当的一级结构特征，并确定第2位残基为异亮氨酸，第5/8位残基为亮氨酸。激肽抑制素代表了一种来自两栖动物皮肤的新型肽原型。
