A simple procedure for the photoregulation of chymotrypsin activity.
Stephen Thompson, Marie-Claude Fawcett, Lesley B Pulman, Colin H Self
文献索引:Photochem. Photobiol. Sci. 5(3) , 326-30, (2006)
全文:HTML全文
摘要
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.
相关化合物
相关文献:
2015-01-02
[ChemBioChem. 16(1) , 83-90, (2014)]
2015-08-01
[Food Funct. 6 , 2626-35, (2015)]
2012-07-01
[Anal. Bioanal. Chem 403(9) , 2655-63, (2012)]
1999-10-20
[Biotechnol. Bioeng. 65(2) , 170-5, (1999)]
2000-02-01
[J. Immunol. 164(3) , 1588-94, (2000)]