Hoskin F C
Biochem Pharmacol. 1985 Jun 15;34(12):2069-72. doi: 10.1016/0006-2952(85)90396-x.
Mipafox, N,N'-diisopropylphosphordiamidofluoridate, has been found to be a reversible competitive inhibitor of a diisopropyl phosphorofluoridate hydrolyzing enzyme (DFPase) isolated from hog kidney and Escherichia coli. Heretofore, this DFPase was characterized by its more rapid hydrolysis of Soman (1,2,2-trimethylpropyl methylphosphonofluoridate), its stimulation by Mn2+, and its wide distribution. In sharp contrast, Mipafox did not inhibit the DFPase found only in cephalopod nerve, hepatopancreas, and saliva, and further characterized by its more rapid hydrolysis of DFP than of Soman, and its indifference to Mn2+. Neither of these two DFPases hydrolyzed Mipafox.
丙氟磷（N，N'-二异丙基磷酰二氟胺）已被发现是从猪肾和大肠杆菌中分离出的二异丙基磷酰氟水解酶（DFPase）的可逆竞争性抑制剂。在此之前，这种DFPase的特点是对梭曼（1,2,2-三甲基丙基甲基磷酰氟）的水解速度更快，受Mn2+刺激，且分布广泛。与之形成鲜明对比的是，丙氟磷并不抑制仅在头足类动物神经、肝胰腺和唾液中发现的DFPase，该酶的特点是对DFP的水解速度比对梭曼更快，且对Mn2+不敏感。这两种DFPase都不能水解丙氟磷。
