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Issue 3, 2006
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A simple procedure for the photoregulation of chymotrypsin activity

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Abstract

A convenient and rapid method for the photo-regulation of the proteolytic enzyme α-chymotrypsin is described. When α-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 α-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.

Graphical abstract: A simple procedure for the photoregulation of chymotrypsin activity

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Publication details

The article was received on 25 Oct 2005, accepted on 09 Jan 2006 and first published on 19 Jan 2006


Article type: Paper
DOI: 10.1039/B515146E
Citation: Photochem. Photobiol. Sci., 2006,5, 326-330
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    A simple procedure for the photoregulation of chymotrypsin activity

    S. Thompson, M. Fawcett, L. B. Pulman and C. H. Self, Photochem. Photobiol. Sci., 2006, 5, 326
    DOI: 10.1039/B515146E

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