Linked Life Data

7510002

Source:http://linkedlifedata.com/resource/pubmed/id/7510002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1994-4-4
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0160-2446
pubmed:author
pubmed:issnType
Print
pubmed:volume
22 Suppl 8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S69-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Rapid inactivation of endothelin-1 by a carboxypeptidase-like enzyme purified from rat kidney.
pubmed:affiliation
Research Department, Ciba-Geigy Corp., Summit, New Jersey 07901.
pubmed:publicationType
Journal Article, In Vitro