title: On the stability of a tumour cell surface protease after exposure to 6N HCl.
abstract: Well defined acinar tumour cells in frozen sections were exposed to 6NHCl for 5 h at room temperature. A technique was designed to monitor the activity of the enzyme, guanidinobenzoatase (GB), on these tumour cells; this involved cross-linking the enzyme to the cell surface and challenging the active centre with known fluorescent probes which only bind to the functional enzyme. It was demonstrated that the enzymic activity can be regained by appropriate folding of the protein.
authors.affiliation: Division of Biochemistry, School of Biological Sciences, University of Manchester, UK.
authors.forename: F S
authors.initials: FS
authors.lastname: Steven
authors.forename: J
authors.initials: J
authors.lastname: Denton
mesh_terms: D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D010450:Endopeptidases / Q000737:chemistry*; D004795:Enzyme Stability; D006801:Humans; D006851:Hydrochloric Acid / Q000494:pharmacology; D009369:Neoplasms / Q000201:enzymology*; D017510:Protein Folding
chemical_list: D002265:Carboxylic Ester Hydrolases; C037288:guanidinobenzoate esterase; D010450:Endopeptidases; D006851:Hydrochloric Acid