Seidah N G, Lazure C, Chrétien M, Thibault G, Garcia R, Cantin M, Genest J, Nutt R F, Brady S F, Lyle T A
Proc Natl Acad Sci U S A. 1984 May;81(9):2640-4. doi: 10.1073/pnas.81.9.2640.
A substance called atrial natriuretic factor (ANF), localized in secretory granules of atrial cardiocytes, was isolated as four homologous natriuretic peptides from homogenates of rat atria. The complete sequence of the longest form showed that it is composed of 33 amino acids. The three other shorter forms (2-33, 3-33, and 8-33) represent amino-terminally truncated versions of the 33 amino acid parent molecule as shown by analysis of sequence, amino acid composition, or both. The proposed primary structure agrees entirely with the amino acid composition and reveals no significant sequence homology with any known protein or segment of protein. The short form ANF-(8-33) was synthesized by a multi-fragment condensation approach and the synthetic product was shown to exhibit specific activity comparable to that of the natural ANF-(3-33).
一种名为心房利钠因子（ANF）的物质定位于心房心肌细胞的分泌颗粒中，从大鼠心房匀浆中分离出四种同源利钠肽。最长形式的完整序列表明它由33个氨基酸组成。其他三种较短形式（2 - 33、3 - 33和8 - 33）通过序列分析、氨基酸组成分析或两者分析表明，它们是33个氨基酸母体分子的氨基末端截短版本。所提出的一级结构与氨基酸组成完全一致，并且与任何已知蛋白质或蛋白质片段均无明显的序列同源性。短形式的ANF -（8 - 33）通过多片段缩合方法合成，合成产物显示出与天然ANF -（3 - 33）相当的比活性。
