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. 1969 Nov;64(3):1103–1106. doi: 10.1073/pnas.64.3.1103

PHOTOREGULATION OF BIOLOGICAL ACTIVITY BY PHOTOCROMIC REAGENTS, II. INHIBITORS OF ACETYLCHOLINESTERASE*,†

Joseph Bieth 1, Spyros M Vratsanos 1, Norbert Wassermann 1, Bernard F Erlanger 1
PMCID: PMC223349  PMID: 5264140

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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