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海岛矛头蝮蛇毒中缓激肽增强肽的一级结构和生物活性

Primary structure and biological activity of bradykinin potentiating peptides from Bothrops insularis snake venom.

作者信息

Cintra A C, Vieira C A, Giglio J R

机构信息

Departamento de Bioquímica, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Brasil.

出版信息

J Protein Chem. 1990 Apr;9(2):221-7. doi: 10.1007/BF01025312.

Abstract

Several bradykinin potentiating peptides (BPPs) were isolated from the venom of the Brazilian arboricole snake Bothrops insularis by gel filtration on Sephadex G-150-120, followed by sequencial high-voltage paper electrophoreses at pH 3.5, 6.5, and 2.1. The BPPs were assayed by their ability to potentiate the contractile activity, on the isolated guinea pig ileum, and the hypotensive activity, on anesthetized rats, of bradykinin. Eight BPPs, containing 3-13 amino acid residues, were sequenced and their primary structures were shown to have a marked degree of homology with those of several BPPs from other venoms.

摘要

通过在Sephadex G - 150 - 120上进行凝胶过滤,随后在pH值为3.5、6.5和2.1条件下依次进行高压纸电泳,从巴西树栖蛇岛矛头蝮(Bothrops insularis)的毒液中分离出了几种缓激肽增强肽(BPPs)。通过检测这些BPPs增强缓激肽对豚鼠离体回肠的收缩活性以及对麻醉大鼠的降压活性的能力来对其进行分析。对8种含有3 - 13个氨基酸残基的BPPs进行了测序,结果表明它们的一级结构与其他毒液中的几种BPPs具有显著的同源性。

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