Monoamine oxidase (MAO-B) activity in liver homogenates and mitochondr
ia from control and B-12-deficients rats was studied under various fun
ctional states of the mitochondria. Preincubation of preparations at 3
2 degrees C increased MAO affinity for benzylamine for control but not
for vitamin B-12-deficient rats. Addition of succinate to the incubat
ion medium was accompanied by a decrease in K-m and an increase in V-m
ax in both groups of animals. Under vitamin B-12 deficiency a correlat
ion between decreased MAO-B activity, decreased succinate oxidation ra
te, and decreased transmembrane potential was found.