Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8396212rdf:typepubmed:Citationlld:pubmed
pubmed-article:8396212lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:8396212lifeskim:mentionsumls-concept:C0006104lld:lifeskim
pubmed-article:8396212lifeskim:mentionsumls-concept:C1998793lld:lifeskim
pubmed-article:8396212lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:8396212pubmed:issue7lld:pubmed
pubmed-article:8396212pubmed:dateCreated1993-10-4lld:pubmed
pubmed-article:8396212pubmed:abstractTextA soluble tripeptidylaminopeptidase has been isolated from human post-mortem cerebral cortex by anion exchange, hydrophobic interaction and size-exclusion chromatography. From gel filtration studies the active enzyme can exist in both high molecular weight (M(r) > 10(6) and smaller forms. The enzyme hydrolyses Ala-Ala-Phe-7-amido-4-methylcoumarin with a pH optimum of around 7.5 and Km of 148 microM. It did not hydrolyse N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, aminoacyl- or dipeptidyl-7-amido-methylcoumarins and was not inhibited by bestatin. The enzyme was inhibited by phenylmethylsulphonyl-fluoride, 3,4-dichloroisocoumarin, N-hydroxymercuriphenyl-sulphonic acid and N-ethylmaleimide showing that its activity is serine and cysteine dependent. The purified enzyme released tripeptides from several naturally occurring neuropeptides with quite broad specificity. Cholecystokinin octapeptide, angiotensin III and neurokinin A were the most rapidly hydrolysed. Peptides with Pro residues around the point of cleavage were not hydrolysed.lld:pubmed
pubmed-article:8396212pubmed:languageenglld:pubmed
pubmed-article:8396212pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:citationSubsetIMlld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8396212pubmed:statusMEDLINElld:pubmed
pubmed-article:8396212pubmed:monthJullld:pubmed
pubmed-article:8396212pubmed:issn0364-3190lld:pubmed
pubmed-article:8396212pubmed:authorpubmed-author:WilsonCClld:pubmed
pubmed-article:8396212pubmed:authorpubmed-author:McDermottJ...lld:pubmed
pubmed-article:8396212pubmed:authorpubmed-author:GibsonA MAMlld:pubmed
pubmed-article:8396212pubmed:issnTypePrintlld:pubmed
pubmed-article:8396212pubmed:volume18lld:pubmed
pubmed-article:8396212pubmed:ownerNLMlld:pubmed
pubmed-article:8396212pubmed:authorsCompleteYlld:pubmed
pubmed-article:8396212pubmed:pagination743-9lld:pubmed
pubmed-article:8396212pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:meshHeadingpubmed-meshheading:8396212-...lld:pubmed
pubmed-article:8396212pubmed:year1993lld:pubmed
pubmed-article:8396212pubmed:articleTitlePurification and characterization of tripeptidylpeptidase-II from post-mortem human brain.lld:pubmed
pubmed-article:8396212pubmed:affiliationMRC Neurochemical Pathology Unit, Newcastle General Hospital, United Kingdom.lld:pubmed
pubmed-article:8396212pubmed:publicationTypeJournal Articlelld:pubmed
entrez-gene:7174entrezgene:pubmedpubmed-article:8396212lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8396212lld:pubmed