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pubmed-article:7510002pubmed:abstractTextA 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
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pubmed-article:7510002pubmed:articleTitleRapid inactivation of endothelin-1 by a carboxypeptidase-like enzyme purified from rat kidney.lld:pubmed
pubmed-article:7510002pubmed:affiliationResearch Department, Ciba-Geigy Corp., Summit, New Jersey 07901.lld:pubmed
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