pubmed-article:7510002 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7510002 | lifeskim:mentions | umls-concept:C0079281 | lld:lifeskim |
pubmed-article:7510002 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:7510002 | lifeskim:mentions | umls-concept:C1882714 | lld:lifeskim |
pubmed-article:7510002 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:7510002 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
pubmed-article:7510002 | pubmed:dateCreated | 1994-4-4 | lld:pubmed |
pubmed-article:7510002 | pubmed:abstractText | A survey of various rat tissues showed that the kidney had the highest endothelin degradation enzyme activity. An enzyme that effectively inactivated endothelin-1 was purified from soluble kidney extracts. This enzyme appeared to contain two subunits with molecular weights of 34 kDa and 21 kDa. It displayed carboxypeptidase-like properties and cleaved off the carboxyl terminal tryptophan of endothelin-1. These results agree with the findings that endothelin-1 is cleared efficiently by the kidney and suggest that this enzyme plays a role in the homeostasis of circulating endothelin-1. | lld:pubmed |
pubmed-article:7510002 | pubmed:language | eng | lld:pubmed |
pubmed-article:7510002 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7510002 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7510002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7510002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7510002 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7510002 | pubmed:issn | 0160-2446 | lld:pubmed |
pubmed-article:7510002 | pubmed:author | pubmed-author:JengA YAY | lld:pubmed |
pubmed-article:7510002 | pubmed:author | pubmed-author:DengYY | lld:pubmed |
pubmed-article:7510002 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7510002 | pubmed:volume | 22 Suppl 8 | lld:pubmed |
pubmed-article:7510002 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7510002 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7510002 | pubmed:pagination | S69-72 | lld:pubmed |
pubmed-article:7510002 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7510002 | pubmed:meshHeading | pubmed-meshheading:7510002-... | lld:pubmed |
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pubmed-article:7510002 | pubmed:meshHeading | pubmed-meshheading:7510002-... | lld:pubmed |
pubmed-article:7510002 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:7510002 | pubmed:articleTitle | Rapid inactivation of endothelin-1 by a carboxypeptidase-like enzyme purified from rat kidney. | lld:pubmed |
pubmed-article:7510002 | pubmed:affiliation | Research Department, Ciba-Geigy Corp., Summit, New Jersey 07901. | lld:pubmed |
pubmed-article:7510002 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7510002 | pubmed:publicationType | In Vitro | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7510002 | lld:pubmed |