Beinfeld M C
Peptides. 1985 Sep-Oct;6(5):857-60. doi: 10.1016/0196-9781(85)90314-6.
Utilizing an antiserum raised against a peptide fragment identical to part of the carboxyl terminal extension of cholecystokinin (CCK) predicted by the sequence of CCK mRNA [7], an antiserum has been generated which does not detect CCK 39, CCK 33, CCK 8, CCK 4 or gastrin 171. This antiserum detects several peptides in rat brain, one similar in size to CCK 33 and another slightly larger than CCK 8. These peptides may represent carboxyl-terminally extended forms of CCK, though their chemical structure has not been determined. These peptides are present in all brain regions where CCK 8 can be detected. The abundance of these peptides, their localization in CCK terminal regions, and their enrichment in synaptosome preparations [1] imply that the tryptic cleavage and amidation reaction occur late in the processing of CCK (as has been observed for other biologically active peptides), and probably occur in the synaptic vesicle.
利用针对胆囊收缩素（CCK）mRNA序列预测的与CCK羧基末端延伸部分相同的肽片段产生的抗血清，已生成一种抗血清，该抗血清无法检测到CCK 39、CCK 33、CCK 8、CCK 4或胃泌素171。这种抗血清在大鼠脑中检测到几种肽，一种大小与CCK 33相似，另一种比CCK 8略大。这些肽可能代表CCK的羧基末端延伸形式，尽管它们的化学结构尚未确定。这些肽存在于所有可检测到CCK 8的脑区。这些肽的丰度、它们在CCK末端区域的定位以及它们在突触体制剂中的富集[1]表明，胰蛋白酶切割和酰胺化反应在CCK加工过程的后期发生（正如在其他生物活性肽中观察到的那样），并且可能发生在突触小泡中。
