Emanuelli M, Raffaelli N, Amici A, Balducci E, Natalini P, Ruggieri S, Magni G
Istituto di Biochimica, Facoltà di Medicina e Chirurgia, Università di Ancona, Italy.
Biochem Pharmacol. 1995 Feb 14;49(4):575-9. doi: 10.1016/0006-2952(94)00478-5.
Nicotinamide mononucleotide (NMN) adenylyltransferase (EC 2.7.7.1) from human placenta is rapidly inactivated by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU). A similar inactivation is observed with other C- and N-nitroso compounds. The inactivation by BCNU is dependent on incubation time, temperature and BCNU concentration. Protective reagents for -SH groups, dithiothreitol and beta-mercaptoethanol, and the substrate NMN are very effective in protecting NMN adenylyltransferase from BCNU inactivation and in preserving its catalytic properties, while ATP is less efficient. Incubation of BCNU-inactivated and dialysed NMN adenylyltransferase with dithiothreitol results in a partial recovery of the enzymatic activity.
