| pubmed-article:6714935 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6714935 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:6714935 | lifeskim:mentions | umls-concept:C0023516 | lld:lifeskim |
| pubmed-article:6714935 | lifeskim:mentions | umls-concept:C0002570 | lld:lifeskim |
| pubmed-article:6714935 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6714935 | pubmed:dateCreated | 1984-6-6 | lld:pubmed |
| pubmed-article:6714935 | pubmed:abstractText | Six aminopeptidases differing in enzymic specificity against various L-amino acid-4-nitroanilides were detected and isolated from the cytosol of leucocytes collected from the buffy coat of human blood. The different enzymes were separated by one step of chromatography on DEAE-Sephacel and were further purified by gel filtration on Sephacryl S-300. The main aminopeptidases of the cytosol were designated aminopeptidases 1, 2, 4 and 5 (AP 1, AP 2, AP 4, AP 5) on the basis of their elution sequence from the first ion-exchange chromatography column on DEAE-Sephacel. Aminopeptidase 1 appeared to be a strongly sulfhydryl-dependent leucine aminopeptidase, activatable by thiol reagents. The enzyme was inhibited by p-chloromercuribenzoate. Its molecular mass was estimated to be 150 kDa. Aminopeptidase 2 showed high specificity for proline-4-nitroanilide. This enzyme was inhibited by p-chloro-mercuribenzoate and bestatin. It exhibited a molecular mass of 70 kDa. Aminopeptidase 4 designated the activities of two different enzymes of apparent molecular masses of 220 and 70 kDa which could be further separated by gel filtration. Aminopeptidase 5 exhibited the properties alike aminopeptidase B with high specific hydrolytic activity against the 4-nitroanilides of lysine and arginine. The molecular mass was estimated to be 90 kDa. Aminopeptidase 3 was a minor component in the cytosol and could be identified as an extracellular leucocyte plasma membrane constituent. The enzyme exhibited properties of a metallo proteinase and could be inhibited by EDTA. The molecular mass was estimated to be 250 kDa. | lld:pubmed |
| pubmed-article:6714935 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6714935 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6714935 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6714935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6714935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6714935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6714935 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6714935 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:6714935 | pubmed:issn | 0018-4888 | lld:pubmed |
| pubmed-article:6714935 | pubmed:author | pubmed-author:TschescheHH | lld:pubmed |
| pubmed-article:6714935 | pubmed:author | pubmed-author:RautenbergWW | lld:pubmed |
| pubmed-article:6714935 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6714935 | pubmed:volume | 365 | lld:pubmed |
| pubmed-article:6714935 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6714935 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6714935 | pubmed:pagination | 49-58 | lld:pubmed |
| pubmed-article:6714935 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:meshHeading | pubmed-meshheading:6714935-... | lld:pubmed |
| pubmed-article:6714935 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6714935 | pubmed:articleTitle | Aminopeptidases from human leucocytes. | lld:pubmed |
| pubmed-article:6714935 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6714935 | lld:pubmed |
