Rouillé Y, Spang A, Chauvet J, Acher R
Laboratory of Biological Chemistry, University of Paris VI, France.
Neuropeptides. 1992 Aug;22(4):223-8. doi: 10.1016/0143-4179(92)90050-7.
A Ca(2+)-dependent endopeptidase cleaving at the carboxyl side of the paired Lys-Arg residues has been found in the neurosecretory granules of the rat neurointermediate pituitary. The specificity pattern on synthetic fluorogenic substrates, the inhibitor profile, the pH optimum of 5.0 and the Ca(2+)-dependence are compatible with an involvement of this enzyme in the prooxytocin and the provasopressin processing within the granules. The enzymatic features of the neurohypophysial granule endopeptidase resemble those of the insulinoma granule type II endopeptidase and suggest that the same Ca(2+)-dependent protease or closely related enzymes could be involved in processing Lys-Arg-containing prohormones in neuroendocrine cells.
在大鼠神经垂体中间叶的神经分泌颗粒中发现了一种依赖钙离子的内肽酶,它在成对的赖氨酸 - 精氨酸残基的羧基侧进行切割。该酶对合成荧光底物的特异性模式、抑制剂谱、5.0的最适pH值以及对钙离子的依赖性,都表明这种酶参与了颗粒内催产素原和加压素原的加工过程。神经垂体颗粒内肽酶的酶学特征与胰岛素瘤颗粒II型内肽酶相似,这表明相同的依赖钙离子的蛋白酶或密切相关的酶可能参与神经内分泌细胞中含赖氨酸 - 精氨酸的激素原的加工过程。