Gluschankof P, Morel A, Benoit R, Cohen P
Biochem Biophys Res Commun. 1985 May 16;128(3):1051-7. doi: 10.1016/0006-291x(85)91046-0.
The products generated after addition of the ARG-LYS esteropeptidase activity purified from rat brain to synthetic somatostatin-28 were analyzed using radioimmunoassay, HPLC and amino acid analysis. In addition to somatostatin-14, both free arginine and free Lysine were identified together with somatostatin-28. The dipeptide ARG-LYS was not present, which indicates that three peptide bonds were hydrolyzed in order to achieve excision of the doublet. Since it is likely that the octacosapeptide is a precursor for both somatostatin-14 and somatostatin-28, these observations add further support to the hypothesis that the convertase is also involved in the in vivo processing of endogenous somatostatin-28.
将从大鼠脑中纯化的精氨酸-赖氨酸酯肽酶活性添加到合成的生长抑素-28后产生的产物，使用放射免疫分析、高效液相色谱和氨基酸分析进行了分析。除了生长抑素-14外，游离的精氨酸和游离的赖氨酸与生长抑素-28一起被鉴定出来。二肽精氨酸-赖氨酸不存在，这表明为了切除双峰，三个肽键被水解。由于八肽很可能是生长抑素-14和生长抑素-28的前体，这些观察结果进一步支持了转化酶也参与内源性生长抑素-28体内加工的假说。
