pubmed-article:8745043 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8745043 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:8745043 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:8745043 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:8745043 | lifeskim:mentions | umls-concept:C0023209 | lld:lifeskim |
pubmed-article:8745043 | lifeskim:mentions | umls-concept:C1000621 | lld:lifeskim |
pubmed-article:8745043 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:8745043 | pubmed:dateCreated | 1996-10-15 | lld:pubmed |
pubmed-article:8745043 | pubmed:abstractText | 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 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 |
pubmed-article:8745043 | pubmed:language | eng | lld:pubmed |
pubmed-article:8745043 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8745043 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8745043 | pubmed:issn | 0196-9781 | lld:pubmed |
pubmed-article:8745043 | pubmed:author | pubmed-author:SalzetMM | lld:pubmed |
pubmed-article:8745043 | pubmed:author | pubmed-author:LaurentVV | lld:pubmed |
pubmed-article:8745043 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8745043 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:8745043 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8745043 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8745043 | pubmed:pagination | 1351-8 | lld:pubmed |
pubmed-article:8745043 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8745043 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8745043 | pubmed:articleTitle | Isolation of a renin-like enzyme from the leech Theromyzon tessulatum. | lld:pubmed |
pubmed-article:8745043 | pubmed:affiliation | Laboratoire de Phylogénie moléculaire des Annélides, ER 87 CNRS, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France. | lld:pubmed |
pubmed-article:8745043 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8745043 | pubmed:publicationType | In Vitro | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8745043 | lld:pubmed |