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pubmed-article:8745043pubmed:abstractTextThis 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 Leu10-Leu11 bond of synthetic porcine angiotensinogen tetradecapeptide yielding the angiotensin I and the Leu11-Val12-Tyr13-Ser14 peptide as products, with a specific activity of 1.35 pmol AI/min/mg (Km 22 microM; Kcat 2.7). The hydrolysis of angiotensinogen is inhibitable at 90% by pepstatin A (IC50 = 4.6 microM), consistent with a renin activity. This is the first biochemical evidence of renin-like enzyme in invertebrates.lld:pubmed
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pubmed-article:8745043pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:8745043pubmed:year1995lld:pubmed
pubmed-article:8745043pubmed:articleTitleIsolation of a renin-like enzyme from the leech Theromyzon tessulatum.lld:pubmed
pubmed-article:8745043pubmed:affiliationLaboratoire de Phylogénie moléculaire des Annélides, ER 87 CNRS, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.lld:pubmed
pubmed-article:8745043pubmed:publicationTypeJournal Articlelld:pubmed
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