Lonovics J, Hajnal F, Mara P, Szabó I, Varró V
Acta Hepatogastroenterol (Stuttg). 1979 Jun;26(3):222-6.
In vitro experiments were carried out to examine the enzymatic activity in various organ homogenates of the dog, which inactivates the biological activity of the synthetic cholecystokinin-octapeptide (CCK-OP). The highest splitting activity was found in the renal cortex; substantially lower activities were registered in the lung, pancreas and small intestine. It seems interesting that neither the gallbladder nor the saliva and the serum contained measurable amount of the CCK-OP splitting activity. An effort was made to characterize the CCK-OP inactivating principle found in the renal cortex. It was ascertained that the CCK-OP was inactivated by a peptidase which is heat sensitive, has a pH optimum of 7,4 and could be inhibited by chelating agents (EDTA) and epsilon-aminocaproic acid. The fact that most of the enzyme function is associated with the sediment obtained at 12 000 g speaks in favour of its mitochondrial origin.
进行了体外实验，以检测犬各种器官匀浆中使合成的胆囊收缩素八肽（CCK-OP）生物活性失活的酶活性。在肾皮质中发现了最高的裂解活性；在肺、胰腺和小肠中记录到的活性明显较低。有趣的是，胆囊、唾液和血清中均未检测到可测量的CCK-OP裂解活性。人们努力对在肾皮质中发现的CCK-OP失活原理进行表征。已确定CCK-OP被一种肽酶失活，该肽酶对热敏感，最适pH为7.4，可被螯合剂（EDTA）和ε-氨基己酸抑制。大多数酶功能与12000g离心得到的沉淀物相关这一事实表明其起源于线粒体。
