Observations on the conformational changes in the structure of a cell surface protease, followed by its ability to be recognised by competitive and non-competitive inhibitors.
Lung tumour cells possess a cell surface protease which can be inhibited by a cytoplasmic protein inhibitor extracted from these cells. The dissociation of this enzyme-inhibitor complex on the surface of tumour cells in sections treated with 10(-4) M sodium dodecyl sulphate has been studied. The dissociation of the inhibitor and regain of enzymic activity was followed by the use of a fluorescent probe which binds to the active centre of the cell surface enzyme in a competitive manner.
Steven
F S
FS
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, UK.
Griffin
M M
MM
Anees
M
M
Benbow
E W
EW
D000585:Aminacrine / Q000378:metabolism; D001667:Binding, Competitive; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002277:Carcinoma / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D005629:Frozen Sections; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D012967:Sodium Dodecyl Sulfate; D013194:Staining and Labeling
D008565:Membrane Proteins; D011480:Protease Inhibitors; D012967:Sodium Dodecyl Sulfate; D000585:Aminacrine; D002265:Carboxylic Ester Hydrolases; C037288:guanidinobenzoate esterase; D010450:Endopeptidases