Abstract
A cDNA encoding a human endothelium-derived vasoconstrictor peptide, endothelin, was isolated from a human placenta cDNA library. The nucleotide sequence of this cDNA clone showed that the primary structure of the human preproendothelin has 212 amino acid residues and is highly homologous to porcine preproendothelin, and that human endothelin is identical with porcine endothelin.
Original language | English (US) |
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Pages (from-to) | 440-444 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 231 |
Issue number | 2 |
DOIs | |
State | Published - Apr 25 1988 |
Keywords
- (Endothelium)
- Cardiovascular physiology
- Endothelin
- Peptide processing
- Vasoconstrictor peptide
- cDNA cloning
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology