ISOLATION OF A RENIN-LIKE ENZYME FROM THE LEECH THEROMYZON TESSULATUM

被引：14

作者：

LAURENT, V

SALZET, M

机构：

[1] Laboratoire de Phylogénie moléculaire des Annélides, ER 87 CNRS, Groupe de Neuroendocrinologie des Hirudinées, SN3, Université des Sciences et Technologies de Lille

来源：

PEPTIDES | 1995年 / 16卷 / 08期

关键词：

ANGIOTENSINOGEN; ANGIOTENSIN I; LEECH; RENIN-ANGIOTENSIN SYSTEM; RENIN-LIKE ENZYME;

D O I：

10.1016/0196-9781(95)02038-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This article reports the purification of a renin-like enzyme (an aspartyl protease) from head parts of the leech Theromyzon tessulatum. After four steps of purification including gel permeation and anion exchange chromatographies followed by reversed-phase HPLC, this enzyme was purified to homogeneity. The renin-like enzyme (of 32 kDa) hydrolyses at neutral pH and at 37 degrees C, the Leu(10)-Leu(11) bond of synthetic porcine angiotensinogen tetradecapeptide yielding the angiotensin I and the Leu(11)-Val(12)-Tyr(13)-Ser(14) peptide as products, with a specific activity of 1.35 pmol AI/min/mg (K-m 22 mu M; K-cat 2.7). The hydrolysis of angiotensinogen is inhibitable at 90% by pepstatin A (IC50 = 4.6 mu M), consistent with a renin activity. This is the first biochemical evidence of renin-like enzyme in invertebrates.

引用

页码：1351 / 1358

页数：8

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