| pubmed-article:3937747 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3937747 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:3937747 | lifeskim:mentions | umls-concept:C0127863 | lld:lifeskim |
| pubmed-article:3937747 | lifeskim:mentions | umls-concept:C1979928 | lld:lifeskim |
| pubmed-article:3937747 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3937747 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:3937747 | pubmed:dateCreated | 1986-4-2 | lld:pubmed |
| pubmed-article:3937747 | pubmed:abstractText | A methionine aminopeptidase (MAP) found in rat liver microsomes behaves as membrane-bound enzyme. Triton-solubilized MAP when chromatographed on DEAE-cellulose columns was separated from other microsomal arylamidases. The enzyme hydrolyzes N-terminal methionine from methionyl-lysyl-bradykinin (Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) being then characterized as a typical aminopeptidase. It also shows preferential arylamidase activity upon Met-2-naphthylamide. MAP was activated by 2-mercaptoethanol and inhibited by p-hydroxymercuribenzoate. Contrarily to other well characterized aminopeptidases, MAP was not affected by EDTA, puromycin or bestatin. Altogether these data suggest that MAP is a unique microsomal enzyme distinct from other previously described aminopeptidases. It could be involved in the removal of methionine from nascent peptides during protein synthesis. | lld:pubmed |
| pubmed-article:3937747 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3937747 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3937747 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3937747 | pubmed:issn | 0020-711X | lld:pubmed |
| pubmed-article:3937747 | pubmed:author | pubmed-author:GuimarãesJ... | lld:pubmed |
| pubmed-article:3937747 | pubmed:author | pubmed-author:FreitasJ... | lld:pubmed |
| pubmed-article:3937747 | pubmed:author | pubmed-author:TermignoniCC | lld:pubmed |
| pubmed-article:3937747 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3937747 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:3937747 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3937747 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3937747 | pubmed:pagination | 1285-91 | lld:pubmed |
| pubmed-article:3937747 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
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| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:meshHeading | pubmed-meshheading:3937747-... | lld:pubmed |
| pubmed-article:3937747 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3937747 | pubmed:articleTitle | Microsomal methionine aminopeptidase: properties of the detergent-solubilized enzyme. | lld:pubmed |
| pubmed-article:3937747 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3937747 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
