표고버섯(L. edodes) 중의 mitochondria는 설탕밀도단계기울기법에 따라 분리정제 하였다. 앞서 보고한 바와 같이, 각 파장별 빛조사(400-700nm)에 따른 mitochondrial ATPase와 ATP synthase의 활성도는 680nm와 470nm에서 각각 활성화되었다. 본 연구에서, 400nm 이하의 파장별 빛조사에 따른 mitochondrial ATPase 및 ATP synthase의 활성도는 380nm와 330nm에서 각각 활성화되었으며, 330nm 및 350에서 각각 억제되었다. FAD의 존재하에서, mitochondrial ATP synthase는 활성화 파장 및 억제 파장의 조사에 의하여 활성도가 각각 증가된 반면, mitochondrial ATPase의 활성도는 감소되었다. 그러나, NADH의 존재하에서, 이들 파장의 조사에 의한 효소의 활성도는 변화가 없었다. 또한, 두 효소는 각각의 활성화 파장 및 억제 파장이 조사됨에 따라 $FADH_2$를 FAD로 산화시키는 spectrum을 보였다. 이로써, 이 두 효소는 빛 조사에 의하여 생체내의 산화 환원반응의 산화제로 작용하였으며, 특히 mitochondrial ATP synthase의 활성화에 따른 광유발물질은 mitochondria 중에 존재하는 flavin 또는 flavoprotein으로 추정된다.
Mitochondria in L. edodes were separated and purified by stepped sucrose density gradient centrifugation. In our previous work, we have found that the activation wavelengths of the mitochondrial ATPase and ATP synthase were 680 nm and 470 nm within the range of 400-700 nm, respectively. The activities of the above enzymes with wavelengths of 300-400 nm region were investigated. The mitochondrial ATPase and ATP synthase were stimulated at 380 nm and 330 nm, respectively, for 30 min illumination compared with dark control group. They, however, were inhibited at 330 nm and 350 nm, respectively. The presence of FAD resulted in inhibition of the activity of the ATPase and stimulation of the activity of the ATP synthase by the activation and inhibition wavelengths. However, the activities of these enzymes were not changed by NADH for the above wavelengths. In the spectral properties, the oxidation of $FADH_2$ into FAD occurs in the presence of the enzymes for illumination of the activation and inhibition wavelengths. Therefore, we can predict that the mitochondrial ATPase and ATP synthase may function as oxidant in the redox reaction by the light illumination and that the light-induced pigment of the mitochondrial ATP synthase should be an oxidized form of a flavoprotein.
