Photoregulation of biological activity by photochromic reagents, IV. A model for diurnal variation of enzymic activity.
Levels of acetylcholinesterase activity can be made to vary in response to the presence or absence of sunlight in a system that can be considered as a model for photoperiodic processes found in nature. The enzyme is rendered photosensitive by the presence of a photochromic inhibitor, N-p-phenylazophenylcarbamyl choline, which changes from a trans to a cis isomer under the influence of the light of the sun and reverts back to the trans isomer in the dark. The two isomers differ in their ability acetylcholinesterase, thus rendering the enzyme system responsive to sunlight. The relationship of this system to photoresponsive processes in nature is discussed, and a possible role in photoregulation is suggested for naturally occurring carotenoids.
D000110:Acetylcholinesterase / Q000528:radiation effects*; D001391:Azo Compounds; D002217:Carbachol; D002940:Circadian Rhythm; D006863:Hydrogen-Ion Concentration; D007202:Indicators and Reagents; D007454:Iodides; D008956:Models, Chemical; D011830:Radiation Effects; D011854:Radiochemistry; D013237:Stereoisomerism; D013472:Sunlight
D001391:Azo Compounds; D007202:Indicators and Reagents; D007454:Iodides; D002217:Carbachol; D000110:Acetylcholinesterase