A simple procedure for the photoregulation of chymotrypsin activity.
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.
Thompson
Stephen
S
Diagnostic and Therapeutic Technologies, School of Clinical and Laboratory Sciences, University of Newcastle upon Tyne, The Medical School, Newcastle upon Tyne, NE2 4HH, UK. C.H.Self@ncl.ac.uk
Fawcett
Marie-Claude
MC
Pulman
Lesley B
LB
Self
Colin H
CH
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000528:radiation effects; D004789:Enzyme Activation / Q000187:drug effects; D000431:Ethanol / Q000031:analogs & derivatives* / Q000494:pharmacology; D015394:Molecular Structure; D009578:Nitrobenzenes / Q000494:pharmacology*; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D010777:Photochemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism; D014443:Tyrosine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D014466:Ultraviolet Rays
D009578:Nitrobenzenes; C011358:Suphepa; D012710:Serum Albumin, Bovine; C063593:1-(2-nitrophenyl)ethanol; C006716:benzoyltyrosine ethyl ester; D000431:Ethanol; D014443:Tyrosine; D010649:Phenylalanine; D002918:Chymotrypsin; C117608:alpha-chymotrypsin