The abiiity of the nicotinamide adenine dinucleotide gl ycohydrolase (NADase) of animal tissues to catalyse an exchange reaction between the nicotinamide moiety of nicotinamide adenine dinucleotide (NAD) and added nicotinarnide has been reported by Za...
The abiiity of the nicotinamide adenine dinucleotide gl ycohydrolase (NADase) of animal tissues to catalyse an exchange reaction between the nicotinamide moiety of nicotinamide adenine dinucleotide (NAD) and added nicotinarnide has been reported by Zatman' Kaplan and Colowick, and the evidence was presented for the formation, by the "insensitive" NADases, of an isonicotinic acid hydrazide (INH) analogue of NAD in which the nicotizzmide moiety of the NAD had been replaced by INH.
In the present paper, the formation of INH analogue of NAD within the tissues from "INH insensitive" animal sources i.e., liver. kidney, heart, lung, muscle and brain, was studied. Mice were injected intraperitoneaily with 500mg. per kilo of nicotinamide 13 hours prior to the injection of INH.
The results were as follows:
1. It has been shown that the administration of INH into mice pretreated with nicotinamide leads to the formation of IINH analogue of NAD in the animal tissues.
2. The highest level of the INH analogue of NAD in mice liver occurred 5 to 10 minutes after the injections of INH, and reached a level of 2.6 micromoles per gram of wet weight liver, that is about 70 percent of the maximal NAD content resulted from nicotinamide pre-treatment.
The synthesis in vivo of INH analogue showed a sharp optimum at a dose of 10 mg. per capita of INH.
3. In the kidney and heart, the formation of INK analogue of NAD was less effective than that of liver.
4. Synthesis in vivo of INH analogue of NAD in the lung, muscle and brain was far less effective than that The levels are 0.6 and 0.5 micromole, respectively. of liver, and the amounts of INH formed were 0.3, 0.2 and 0.18 micromole, respectively.