Garcia R, Thibault G, Seidah N G, Lazure C, Cantin M, Genest J, Chrétien M
Biochem Biophys Res Commun. 1985 Jan 16;126(1):178-84. doi: 10.1016/0006-291x(85)90588-1.
The effect of the length of ANF peptides on the inhibition of the norepinephrine-induced contraction was studied. Starting from the 26 residues ANF (Arg101-Tyr126), shorter N- and/or C-terminal fragments were produced, either by N-terminal chemical cleavage or C-terminal enzymatic digestion of ANF or both respectively. The N-terminal removal of Arg101 did not modify the inhibitory response. Further N-terminal truncation up to des-Arg101-Arg102-Ser103-Ser104 ANF still produced a marked inhibitory effect on norepinephrine. In contrast C-terminal cleavage had a much more pronounced effect. Since des-Tyr126 ANF, des-Arg125-Tyr126 ANF and des-Phe124-Arg125-Tyr126 ANF exhibit much lower activities than the parent ANF. Finally, when the 5 residues C-terminal to Cys121 are removed, the resulting molecule is almost inactive. These data indicate that the C-terminal segment of ANF may modulate the binding of ANF to its receptor(s). Relatively, the N-terminal region seems to be much less important.
研究了心钠素（ANF）肽段长度对去甲肾上腺素诱导收缩的抑制作用。从26个残基的心钠素（Arg101 - Tyr126）开始，通过心钠素的N端化学裂解或C端酶切或分别进行两者操作，产生了较短的N端和/或C端片段。N端去除Arg101并未改变抑制反应。进一步N端截短直至去-Arg101-Arg102-Ser103-Ser104心钠素对去甲肾上腺素仍有显著抑制作用。相比之下，C端裂解的影响更为显著。因为去-Tyr126心钠素、去-Arg125-Tyr126心钠素和去-Phe124-Arg125-Tyr126心钠素的活性比母体心钠素低得多。最后，当去除Cys121 C端的5个残基时，所得分子几乎无活性。这些数据表明心钠素的C端片段可能调节心钠素与其受体的结合。相对而言，N端区域似乎不太重要。
