The isolation of angiotensin-converting enzyme cDNA

K. E. Bernstein, B. M. Martin, E. A. Bernstein, J. Linton, L. Striker, G. Striker

Research output: Contribution to journalArticlepeer-review

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Abstract

Angiotensin-converting enzyme (ACE) is an Zn(II)-containing dipeptidyl carboxypeptidase that converts angiotensin I to the potent vasoconstrictor, angiotensin II. Using oligonucleotide probes based on the amino acid sequence of mouse kidney ACE, cDNA encoding this protein has been isolated. One cDNA, ACE.31, encodes the N-terminal 332 amino acids of mouse ACE, a portion of the protein containing a putative 34-amino acid leader sequence and the N terminus of the mature protein. Northern analyses with cloned ACE cDNA revealed that both mouse kidney and lung express two ACE mRNAs, one of 4900 and another of 4150 bases. Southern analysis suggests that cDNA ACE.31 is the product of a single gene, and thus these data add evidence to the hypothesis that the converting enzymes produced by epithelial and endothelial cells are identical.

Original languageEnglish
Pages (from-to)11021-11024
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number23
StatePublished - 1988
Externally publishedYes

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