ADENOSINE TRIPHOSPHATASE AND ALCOHOL DEHYDROGENASE ACTIVITY IN THE VISUAL CELL OUTER SEGMENT(Symposium on Histochemistry of the Sensory Organs)

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The albino rat retina was treated by 1% digitonin solution and electronmicroscopy was performed. ATPase activity in the outer segment did not appeared to be influenced by the digitonin treatment. Electrophoresis indicated that the outer segment lees kept a conspicuous ATPase activity but rhodopsin band was free from ATPase activity. Biochemical assay demonstrated that ATPase activity in the outer segment highly depended on Na and K ions. The homogenate of the frog retina showed a high dehydrogenase activity to retinol as a substrate, but a very low activity to ethanol. ADH activity was histochemically detected in the outer segment on an albino rat retina and optimal pH of phosphate buffer for the tissue reaction seemed to be between 7.8-8.0 than 7.4. Electronmicroscopically formazan deposit was detected on the electron dense layer of the outer segment lamellae. Formazan deposit of ten arranged to surround a disc of about 50 Å in diameter on the electron dense layer.
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