Burbach J P, Terwel D, Lebouille J L
Biochem Biophys Res Commun. 1987 Apr 29;144(2):726-31. doi: 10.1016/s0006-291x(87)80025-6.
The aminopeptidase activity in the brain which converts vasopressin into centrally active metabolites, was quantitated on basis of the release of 3H-Phe from the substate [3H-Phe3]vasopressin and separation by hydrophobic interaction chromatography on mini-columns. After subcellular fractionation of whole rat brain homogenates the highest specific activity of the peptidase was recovered in membrane fractions, in particular microsomes and the P3 fraction, and the cytosol. The peptidase activity was present in all brain areas. Highest activity was measured in membranes of the bulbus olfactorius, preoptical area and cerebellum. Lowest activity was found in the medulla oblongata and striatum. The peptidase activity is not restricted to the vasopressin system per se, but may have a more general role in neuropeptide metabolism.
大脑中可将血管加压素转化为具有中枢活性代谢物的氨肽酶活性，是根据底物[3H - 苯丙氨酸3]血管加压素释放出3H - 苯丙氨酸，并通过微型柱上的疏水相互作用色谱法进行分离来定量的。对全大鼠脑匀浆进行亚细胞分级分离后，肽酶的最高比活性在膜组分中回收，特别是微粒体和P3组分以及胞质溶胶中。肽酶活性存在于所有脑区。在嗅球、视前区和小脑的膜中测得的活性最高。在延髓和纹状体中发现的活性最低。肽酶活性并不局限于血管加压素系统本身，而是可能在神经肽代谢中具有更普遍的作用。
