Cloning and sequence analysis of cDNA encoding the precursor of a human endothelium‐derived vasoconstrictor peptide, endothelin: identity of human and porcine …
Y Itoh, M Yanagisawa, S Ohkubo, C Kimura… - FEBS …, 1988 - Wiley Online Library
Y Itoh, M Yanagisawa, S Ohkubo, C Kimura, T Kosaka, A Inoue, N Ishida, Y Mitsui, H Onda…
FEBS letters, 1988•Wiley Online LibraryA 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.
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.
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.
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