Amino acid sequence and relative biological activity of eel atrial natriuretic peptide.
A peptide exhibiting vasodepressor and natriuretic activities in rats was isolated from eel atria, and its primary structure was determined as H-Ser-Lys-Ser-Ser-Ser-Pro-Cys-Phe-Gly-Gly-Lys-Leu-Asp-Arg-Ile-Gly-Ser-Tyr-Ser- Gly-Leu-Gly-Cys-Asn-Ser-Arg-Lys-OH. This peptide, termed eel atrial natriuretic peptide (ANP), has sequence homology of 59% to mammalian (human or rat) ANP, 52% to fowl ANP, and 46% to frog ANP. When the biological activity of synthetic eel ANP was compared with that of human ANP, the eel peptide was 110 times more potent for the vasodepressor activity in eels, nearly equipotent for the vasodepressor activity in quails, and 20 times less potent for the vasodepressor and natriuretic activity in rats.
Takei
Y
Y
Department of Physiology, Kitasato University School of Medicine, Kanagawa, Japan.
Takahashi
A
A
Watanabe
T X
TX
Nakajima
K
K
Sakakibara
S
S
D000595:Amino Acid Sequence; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000138:chemical synthesis / Q000378:metabolism* / Q000652:urine; D002852:Chromatography, Ion Exchange; D004524:Eels; D006801:Humans; D008969:Molecular Sequence Data; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D009320:Atrial Natriuretic Factor