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On the stability of a tumour cell surface protease after exposure to 6N HCl.
Steven, F S; Denton, J.
Affiliation
  • Steven FS; Division of Biochemistry, School of Biological Sciences, University of Manchester, UK.
Anticancer Res ; 17(2A): 891-3, 1997.
Article in En | MEDLINE | ID: mdl-9137423
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.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Carboxylic Ester Hydrolases / Neoplasms Limits: Humans Language: En Journal: Anticancer Res Year: 1997 Document type: Article Affiliation country: United kingdom Publication country: GR / GRECIA / GREECE / GRÉCIA
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Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Carboxylic Ester Hydrolases / Neoplasms Limits: Humans Language: En Journal: Anticancer Res Year: 1997 Document type: Article Affiliation country: United kingdom Publication country: GR / GRECIA / GREECE / GRÉCIA