Diabetes and adenosine triphosphatase: the effects of insulin, thyroxin and inhibitors on atpase

ABSTRACT

The enzyme ATPase was obtained from liver mitochondria of normal [N] and alloxan diabetic [D] rabbits. Results of the present study show that diabetes inhibited DNP-stimulated ATPase activity [40%].Insulin had no effect on the enzyme activity in N rabbits, but restored it to normal level in D animals. Thyroxine administered in vivo increased ATPase activity in both N [55%]and D [50%] rabbits. However, thiouracill given orally decreased enzyme activity in N [45%] and in D [32%] rabbits, but the enzyme activity is restored to normal level after treatment with thyroxine. The effect of some inhibitors of adenine nucleotide translocase on ATPase were carried out, it was found that, the enzyme activity is inhibited in N and D rabbits by sulfobromophthalein [I [50]; N = 12,D = 6 n mol/mg protein]; agaric acid [I[50]; N > 40,D = 25 n mol/mg protein]; hexachlorophene, 12 n mol/mg protein inhibited the enzyme activity [47% in N and 28% in D]. However, 2-p-chlorophenyl-4 [3,4-dihydroxy-phenyl]- thiazole is a weak inhibitor