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Title: A simple procedure for the photoregulation of chymotrypsin activity. Author: Thompson S, Fawcett MC, Pulman LB, Self CH. Journal: Photochem Photobiol Sci; 2006 Mar; 5(3):326-30. PubMed ID: 16520868. 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.[Abstract] [Full Text] [Related] [New Search]