Matsas R, Turner A J, Kenny A J
FEBS Lett. 1984 Sep 17;175(1):124-8. doi: 10.1016/0014-5793(84)80583-9.
Endopeptidase-24.11 (EC 3.4.24.11) from pig kidney hydrolysed CCK-8 (sulphated) at two distinct sites: Asp-Tyr(SO3H)-Met-Gly Trp-Met-Asp PheNH2. Under initial conditions, the splitting of the Asp7-Phe8NH2 bond proceeded 4-times more rapidly than the Gly4-Trp5 bond. Pig brain striatal synaptic membranes attacked this substrate at the same sites and this activity was inhibited by phosphoramidon. However, other products were detected even in the presence of phosphoramidon. One of these products was identified as free tryptophan. Since their formation was inhibited by bestatin, one or more membrane aminopeptidases is also implicated in the degradation of CCK-8.
猪肾中的内肽酶-24.11（EC 3.4.24.11）在两个不同位点水解CCK-8（硫酸化型）：天冬氨酸-酪氨酸（SO3H）-甲硫氨酸-甘氨酸-色氨酸-甲硫氨酸-天冬氨酸-苯丙氨酸NH2。在初始条件下，天冬氨酸7-苯丙氨酸8NH2键的断裂速度比甘氨酸4-色氨酸5键快4倍。猪脑纹状体突触膜在相同位点攻击该底物，且该活性被膦甲脒抑制。然而，即使存在膦甲脒，仍检测到其他产物。其中一种产物被鉴定为游离色氨酸。由于其形成被贝司他汀抑制，一种或多种膜氨基肽酶也参与了CCK-8的降解。
