McDermott J R, Biggins J A, Smith A I, Gibson A M, Keith A B, Edwardson J A
MRC Neuroendocrinology Unit, Newcastle General Hospital.
Peptides. 1988 Jul-Aug;9(4):757-61. doi: 10.1016/0196-9781(88)90118-0.
The major product on incubation of CLIP (ACTH18-39) with rat and mouse serum, rat plasma and whole blood, and soluble extracts of rat pituitary is [des-Arg1]-CLIP (ACTH19-39) while [des-Phe22]-CLIP (ACTH18-38) is the major product with pituitary particulate fraction. In both cases, p-chloromercuribenzoate-sensitive, metal-dependent peptidase activity appears to be responsible for the cleavage. The serum enzyme may be related to proline aminopeptidase. Material coeluting with [des-Arg]-CLIP on two HPLC solvent gradients is present in the superfusion media from neurointermediate lobes of genetically obese (ob/ob) mice but is not present in acid extracts of the lobe. This suggests that postsecretory processing of CLIP may involve removal of the N-terminal Arg residue.
将CLIP（促肾上腺皮质激素18 - 39）与大鼠和小鼠血清、大鼠血浆和全血以及大鼠垂体的可溶性提取物一起温育时，主要产物是[去-精氨酸1]-CLIP（促肾上腺皮质激素19 - 39），而[去-苯丙氨酸22]-CLIP（促肾上腺皮质激素18 - 38）是垂体微粒体部分的主要产物。在这两种情况下，对氯汞苯甲酸敏感的、金属依赖性肽酶活性似乎负责这种裂解。血清酶可能与脯氨酸氨肽酶有关。在两种高效液相色谱溶剂梯度上与[去-精氨酸]-CLIP共洗脱的物质存在于遗传性肥胖（ob/ob）小鼠神经中间叶的灌流介质中，但不存在于该叶的酸提取物中。这表明CLIP的分泌后加工可能涉及N端精氨酸残基的去除。
