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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1996-10-15
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0196-9781
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1351-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8745043-Amino Acid Sequence,
pubmed-meshheading:8745043-Angiotensin I,
pubmed-meshheading:8745043-Angiotensin II,
pubmed-meshheading:8745043-Angiotensinogen,
pubmed-meshheading:8745043-Animals,
pubmed-meshheading:8745043-Aspartic Acid Endopeptidases,
pubmed-meshheading:8745043-Binding Sites,
pubmed-meshheading:8745043-Humans,
pubmed-meshheading:8745043-Hydrogen-Ion Concentration,
pubmed-meshheading:8745043-Leeches,
pubmed-meshheading:8745043-Molecular Sequence Data,
pubmed-meshheading:8745043-Molecular Weight,
pubmed-meshheading:8745043-Peptides,
pubmed-meshheading:8745043-Rats,
pubmed-meshheading:8745043-Renin,
pubmed-meshheading:8745043-Substrate Specificity,
pubmed-meshheading:8745043-Swine,
pubmed-meshheading:8745043-Temperature
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pubmed:year |
1995
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pubmed:articleTitle |
Isolation of a renin-like enzyme from the leech Theromyzon tessulatum.
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pubmed:affiliation |
Laboratoire de Phylogénie moléculaire des Annélides, ER 87 CNRS, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
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pubmed:publicationType |
Journal Article,
In Vitro
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