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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-12-23
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pubmed:abstractText |
We have identified on the membranes of the locomotory muscle of Ascaris suum an amastatin-sensitive aminopeptidase that hydrolyses the bioactive neuropeptides AF1 (KNEFIRF-NH2) and AF2 (KHEYLRF-NH2), by cleavage of the Lys1-Asn2 and Lys1-His2 peptide bonds, respectively. AF2 (1.2 nmol of HEYLRF-NH2 formed min[-1] (mg protein[-1])) was hydrolysed at a faster rate compared to AF1 (0.2 nmol of NEFIRF-NH2 formed min[-1] (mg protein[-1])). AF1 hydrolysis by the aminopeptidase was inhibited by the amastatin (IC50, 9.0 microM), leuhistin (IC50, 1.25 microM) but was insensitive to puromycin, indicating a similarity to mammalian aminopeptidase N. The enzyme was also inhibited by arphamenine B (IC50, 9.0 microM), (2S, 3R)-3-amino-2-hydroxy-4-(4-nitrophenyl)butanoyl-L-leucine (IC50, 8.0 microM), bestatin (IC50, 15.0 microM) and 1 mM 1-10 bis-phenanthroline. The detergent Triton X-100 solubilised enzyme had a pI of 5.0 and after 1000-fold purification by ion-exchange chromatography, appeared to have a Mr of around 240,000 by SDS-PAGE. The purified aminopeptidase had a Km of 534 microM for the hydrolysis of AF1 and cleaved Phe1 from FMRF-NH2, but was unable to hydrolyse DFMRF-NH2 or FDMRF-NH2. The aminopeptidase that we have described in this report might have a role in the extracellular metabolism and inactivation of neuropeptides acting on the locomotory muscle of A. suum.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/7-amino-4-methylcoumarin,
http://linkedlifedata.com/resource/pubmed/chemical/AF1 neuropeptide,
http://linkedlifedata.com/resource/pubmed/chemical/AF2 neuropeptide,
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Coumarins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/amastatin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0166-6851
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
225-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9364967-Aminopeptidases,
pubmed-meshheading:9364967-Animals,
pubmed-meshheading:9364967-Anti-Bacterial Agents,
pubmed-meshheading:9364967-Ascaris suum,
pubmed-meshheading:9364967-Cell Membrane,
pubmed-meshheading:9364967-Chromatography, Ion Exchange,
pubmed-meshheading:9364967-Coumarins,
pubmed-meshheading:9364967-Hydrolysis,
pubmed-meshheading:9364967-Isoelectric Point,
pubmed-meshheading:9364967-Kinetics,
pubmed-meshheading:9364967-Molecular Weight,
pubmed-meshheading:9364967-Muscle, Skeletal,
pubmed-meshheading:9364967-Neuropeptides,
pubmed-meshheading:9364967-Peptides,
pubmed-meshheading:9364967-Protease Inhibitors,
pubmed-meshheading:9364967-Solubility
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pubmed:year |
1997
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pubmed:articleTitle |
Purification and properties of a membrane aminopeptidase from Ascaris suum muscle that degrades neuropeptides AF1 and AF2.
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pubmed:affiliation |
Department of Pure and Applied Biology, University of Leeds, UK.
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pubmed:publicationType |
Journal Article
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