Miyata A, Minamino N, Kangawa K, Matsuo H
Department of Biochemistry, Miyazaki Medical College, Japan.
Biochem Biophys Res Commun. 1988 Sep 30;155(3):1330-7. doi: 10.1016/s0006-291x(88)81287-7.
Morphological and pharmacological observations have suggested that chicken atrial natriuretic peptide (ANP) is different from mammalian ANP. The present survey for the as yet unidentified ANP in chicken heart was performed by monitoring the relaxant effect on chick rectum. From the low molecular weight component of rectum relaxant activity observed in acid extracts of chicken ventricle, a novel 29-amino acid peptide was purified. The identical peptide was also isolated from acid extracts of chicken atrium. The peptide elicited a pharmacological spectrum very similar to that of mammalian ANP, including diuretic-natriuretic and hypotensive activity. Thus, the peptide was designated "chicken alpha-ANP (alpha-chANP)". The complete amino acid sequence determined for the peptide showed remarkable homology with that of mammalian alpha-ANP. However, maximum homology was observed when the peptide was compared with a recently identified porcine brain natriuretic peptide (BNP).
形态学和药理学观察表明,鸡心房利钠肽(ANP)与哺乳动物的ANP不同。通过监测对雏鸡直肠的舒张作用,对鸡心脏中尚未鉴定的ANP进行了本次研究。从鸡心室酸提取物中观察到的直肠舒张活性的低分子量组分中,纯化出一种新的29个氨基酸的肽。从鸡心房的酸提取物中也分离出了相同的肽。该肽引发的药理学谱与哺乳动物ANP非常相似,包括利尿排钠和降压活性。因此,该肽被命名为“鸡α-ANP(α-chANP)”。所确定的该肽的完整氨基酸序列与哺乳动物α-ANP的序列具有显著的同源性。然而,当将该肽与最近鉴定的猪脑利钠肽(BNP)进行比较时,观察到了最大同源性。