. Biological structure and function; proceedings. Biochemistry; Cytology. 12 OLOV LINDBERG et ul. It was shown previously that amytal inhibits shghtly the dinitro- phenol-induced ATPase [75], and that this inhibition can be greatly potentiated if a stimulating concentration of atebrin [76] or chlorpromazine [77] is added. Fig. 7 illustrates this effect and shows that a similar poten- tiation did not occur with azide or desaminothyroxine. In fact, des- aminothyroxine seemed even to eliminate the slight inhibition given by log M Fig. 6. Comparison of effects of azide, atebrine, chlorpro
. Biological structure and function; proceedings. Biochemistry; Cytology. 12 OLOV LINDBERG et ul. It was shown previously that amytal inhibits shghtly the dinitro- phenol-induced ATPase [75], and that this inhibition can be greatly potentiated if a stimulating concentration of atebrin [76] or chlorpromazine [77] is added. Fig. 7 illustrates this effect and shows that a similar poten- tiation did not occur with azide or desaminothyroxine. In fact, des- aminothyroxine seemed even to eliminate the slight inhibition given by log M Fig. 6. Comparison of effects of azide, atebrine, chlorpromazine and desamino- thyroxine on the dinitrophenol-induced ATPase activity of rat liver mitochondria. Experimental conditions as in Fig. i. An interesting effect of atebrin was discovered by observing that this compound in a concentration of o • 5 mM was able to relieve almost com- pletely the inhibitory effect of desaminothyroxine on the dinitrophenol- induced ATPase reaction (Table I). Peculiarly enough, this effect of atebrin was not shared by chlorpromazine. Similarly, no atebrin-like effect was found with flavin nucleotides. It appeared from the above findings that the effect of desaminothy- roxine on the dinitrophenol-induced ATPase clearly differed from those of the flavin antagonists, whereas the difference from that of azide was less obvious. However, a clear-cut distinction was found also between des- aminothyroxine and azide in the effects of the inhibitors on the Mg + +- activated ATPase of the Kielley and Kielley preparation. As was reported previously [76], the Mg "^ -activated ATPase is characterized by a stimula- tion, up to about 50*)^, by 0"5-i niM sodium dithionite. This compound, however, not only stimulates the Mg + +-activated ATPase reaction but. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resembl
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