Vanhoof G, De Block J, De Meester I, Scharpé S, De Potter W P
Laboratory of Clinical Biochemistry, University of Antwerp, Wilrijk, Belgium.
Neurochem Int. 1992 Sep;21(2):203-8. doi: 10.1016/0197-0186(92)90148-k.
Aminopeptidase P (EC 3.4.11.9) is demonstrated for the first time in the cytosolic fraction of chromaffin cells of the bovine adrenal medulla. The enzyme is inhibited by metal chelators and by sulfhydryl-reactive agents, which suggests that both a tightly bound metal ion and a cysteine residue are necessary for enzymatic activity. Aminopeptidase P might be important for the modulation of the biological activity of neuropeptides. Its occurrence in the adrenal chromaffin cells provides a useful tool for studying the function of this unique proline-specific peptidase in neuropeptide processing and secretion.
氨肽酶P（EC 3.4.11.9）首次在牛肾上腺髓质嗜铬细胞的胞质组分中被证实。该酶受到金属螯合剂和巯基反应性试剂的抑制，这表明紧密结合的金属离子和半胱氨酸残基对于酶活性都是必需的。氨肽酶P可能对神经肽生物活性的调节很重要。它在肾上腺嗜铬细胞中的存在为研究这种独特的脯氨酸特异性肽酶在神经肽加工和分泌中的功能提供了一个有用的工具。
