SKEGGS L T, KAHN J R, LENTZ K, SHUMWAY N P
J Exp Med. 1957 Sep 1;106(3):439-53. doi: 10.1084/jem.106.3.439.
A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently link hypertensin I to the protein renin substrate.
通过对蛋白肾素底物进行胰蛋白酶降解制备的纯化多肽肾素底物制剂,已用氟二硝基苯法进行分析,在用肾素、羧肽酶和异硫氰酸苯酯降解后,发现其具有氨基酸序列:asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser。这些氨基酸中的前10个构成血管紧张素I,它是通过肾素裂解亮氨酰-亮氨酸键而释放的。其余4个氨基酸,leu、val、tyr、ser,显然将血管紧张素I与蛋白肾素底物相连。