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Lookup NU author(s): Dr Stephen Thompson,
Emeritus Professor Colin Self
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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.
Author(s): Thompson S, Fawcett M-C, Pulman LB, Self CH
Publication type: Article
Publication status: Published
Journal: Photochemical and Photobiological Sciences
Print publication date: 01/01/2006
ISSN (print): 1474-905X
ISSN (electronic): 1474-9092
Publisher: Royal Society of Chemistry
PubMed id: 16520868
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