Clamagirand C, Camier M, Fahy C, Clavreul C, Créminon C, Cohen P
Biochem Biophys Res Commun. 1987 Mar 13;143(2):789-96. doi: 10.1016/0006-291x(87)91423-9.
Purified secretory granules from the corpus luteum of super ovulated and fecundated cows, at day 7-8 after the heat period, were used as a source of pro-ocytocin/neurophysin (pro OT/Np) processing enzymes. An endoprotease comparable to the previously described pituitary enzyme both by its catalytic properties and sensitivity to various inhibitors was characterized. This protease cleaves pro OT/Np (1-20) after the basic Lys11Arg12 doublet to release OT Gly10 Lys11 Arg12. Moreover C-terminally extended ocytocin, i.e. OTGlyLys and OTGlyLysArg together with ocytocin were identified in extracts from the corpus luteum. Together these data argue strongly in favor of pro OT/Np processing pathways in which cleavage of the precursor at the Arg12-Ala13 peptide bond is the primary event.
在发情期后第7 - 8天,从超排和受孕母牛的黄体中纯化的分泌颗粒被用作促催产素/神经垂体素(pro OT/Np)加工酶的来源。一种在催化特性和对各种抑制剂的敏感性方面与先前描述的垂体酶相当的内切蛋白酶得到了表征。这种蛋白酶在碱性的Lys11Arg12双联体之后切割pro OT/Np(1 - 20),以释放OT Gly10 Lys11 Arg12。此外,在黄体提取物中鉴定出了C末端延伸的催产素,即OTGlyLys和OTGlyLysArg以及催产素。这些数据共同有力地支持了pro OT/Np加工途径,其中前体在Arg12 - Ala13肽键处的切割是主要事件。