Isolation and characterization of iso-rANP, a new natriuretic peptide from rat atria

T. Geoffrey Flynn, Anoop Brar, Linda Tremblay, Inder Sarda, Christina Lyons, Donald B. Jennings

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Abstract

Using a specific radioimmunoassay we have isolated and sequenced a new 45-amino acid peptide from rat atria which exhibits similar physiological and pharmacological properties to rat atrial natriuretic peptide (rANP). We have termed the new peptide iso-rANP, because of its functional and structural similarities to rANP. Amino acid sequence differences show that iso-rANP is genetically distinct from rANP. Iso-rANP has a single disulfide bond between residues 23-39 and this portion of the peptide shows substantial homology to rANP and to porcine brain natriuretic peptide (BNP). Little homology is evident at the N- and C-termini of iso-rANP and ANP. Iso-rANP is equipotent with rANP in eliciting diuresis, natriuresis and hypotension in the bioassay rat.

Original languageEnglish
Pages (from-to)830-837
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume161
Issue number2
DOIs
StatePublished - Jun 15 1989

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