Abstract:
:The enzymic activity of acetylcholinesterase can be photoregulated through the mediation of photochromic inhibitors of the enzyme. N-p-phenylazophenyl-N-phenylcarbamyl fluoride, an irreversible inhibitor of acetylcholinesterase, exists as two geometric isomers which are interconvertible through the action of light. The cis isomer, which predominates after exposure to light of 320 nm, is more active than the trans isomer, which results from exposure to light of 420 nm. It was possible, therefore, to use light energy to regulate the inactivation of the enzyme. Similarly, levels of acetylcholinesterase activity could be photo-regulated in a completely reversible manner by means of the photochromic reversible inhibitor p-phenylazophenyltrimethylammonium chloride. These experiments can serve as models for similar phenomena observed in nature, particularly in photoperiodic rhythms of higher animals.
journal_name
Proc Natl Acad Sci U S Aauthors
Bieth J,Vratsanos SM,Wassermann N,Erlanger BFdoi
10.1073/pnas.64.3.1103subject
Has Abstractpub_date
1969-11-01 00:00:00pages
1103-6issue
3eissn
0027-8424issn
1091-6490journal_volume
64pub_type
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