De Léan A, Thibault G, Seidah N G, Lazure C, Gutkowska J, Chrétien M, Genest J, Cantin M
Biochem Biophys Res Commun. 1985 Oct 15;132(1):360-7. doi: 10.1016/0006-291x(85)91030-7.
The activity of various fragments of ANF as inhibitors of aldosterone secretion and as competitors of [125I] ANF (Arg101-Tyr126) binding to specific receptors was studied in bovine zona glomerulosa. Shortening or lengthening the N-terminal segment of ANF does not alter its biological activity while minimally altering affinity for its receptor. Removal of the C-terminal to Cys121 or expansion up to Arg128 leads to 1000-fold decrease in receptor affinity and activity. The results indicate the importance of the C-terminal segment of ANF in determining its active conformation.
在牛肾小球带中研究了心房钠尿肽（ANF）各种片段作为醛固酮分泌抑制剂以及作为[125I]ANF（精氨酸101-酪氨酸126）与特异性受体结合的竞争者的活性。缩短或延长ANF的N末端片段不会改变其生物学活性，同时对其受体的亲和力仅有微小改变。去除C末端至半胱氨酸121或扩展至精氨酸128会导致受体亲和力和活性降低1000倍。结果表明ANF的C末端片段在确定其活性构象中具有重要作用。
