光致变色试剂对生物活性的光调节，IV。酶活性日变化的模型。
Photoregulation of biological activity by photochromic reagents, IV. A model for diurnal variation of enzymic activity.
作者信息
Bieth J, Wassermann N, Vratsanos S M, Erlanger B F
出版信息
Proc Natl Acad Sci U S A. 1970 Jul;66(3):850-4. doi: 10.1073/pnas.66.3.850.
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.
在一个可被视为自然界中光周期过程模型的系统中，乙酰胆碱酯酶的活性水平会因有无阳光而发生变化。一种光致变色抑制剂N-对苯基偶氮苯基氨基甲酰胆碱的存在使该酶具有光敏性，这种抑制剂在太阳光的影响下会从反式异构体转变为顺式异构体，并在黑暗中恢复为反式异构体。这两种异构体对乙酰胆碱酯酶的作用不同，从而使酶系统对阳光产生响应。本文讨论了该系统与自然界中光响应过程的关系，并提出天然存在的类胡萝卜素在光调节中可能发挥的作用。
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