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A simple procedure for the photoregulation of chymotrypsin activity

Lookup NU author(s): Dr Stephen Thompson, Marie-claude Fawcett, Emeritus Professor Colin Self

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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. © The Royal Society of Chemistry and Owner Societies 2006.

Publication metadata

Author(s): Thompson S, Fawcett M-C, Pulman LB, Self CH

Publication type: Article

Publication status: Published

Journal: Photochemical and Photobiological Sciences

Year: 2006

Volume: 5

Issue: 3

Pages: 326-330

Print publication date: 01/01/2006

ISSN (print): 1474-905X

ISSN (electronic): 1474-9092

Publisher: Royal Society of Chemistry

URL: http://dx.doi.org/10.1039/b515146e

DOI: 10.1039/b515146e

PubMed id: 16520868

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