A simple procedure for the photoregulation of chymotrypsin activity

Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology
Stephen ThompsonC H Self

Abstract

A convenient and rapid method for the photo-regulation of the proteolytic enzyme alpha-chymotrypsin is described. When alpha-chymotrypsin is coated with photolytic 1-(2-nitrophenyl)ethanol residues this not only markedly reduces the capability of the enzyme to digest both of the small substrates N-benzoyl-L-tyrosine ethyl ester and N-succinyl-L-phenylalanine p-nitroanilide, but also completely inhibits the enzyme's proteolytic activity. The inactivated alpha-chymotrypsin can then be reactivated under physiological conditions, when and where it is required, by exposure to UV-A light. These results further demonstrate that 1-(2-nitrophenyl)ethanol coated proteins can often be used as light sensitive biological switches as a simple alternative to site directed procedures.

References

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May 1, 1995·Biochemical Society Transactions·S ThompsonC H Self
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Jul 9, 2004·Biochemical and Biophysical Research Communications·Laurent BédouetDaniel Thomas

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Citations

Aug 2, 2008·Zhurnal evoliutsionnoĭ biokhimii i fiziologii·S A ZabelinskiĭA I Krivchenko
Jun 28, 2019·Advanced Synthesis & Catalysis·Christiane ClaaßenDörte Rother
Feb 28, 2008·Chemical Reviews·Norbert Hoffmann

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