title: Pressure-induced molten globule state of cholinesterase.
abstract: The denaturing effect of pressure on the structure of human butyrylcholinesterase was examined by gel electrophoresis under pressure and by 8-anilino-1-naphthalene sulfonate (ANS) binding. It was found that the fluorescence intensity of bound ANS is increased by pressure between 0.5 and 1.5 kbar and that the hydrodynamic volume of the enzyme swells when pressures around 1.5 kbar are applied. These findings indicate that pressure denaturation of butyrylcholinesterase is a multi-step process and that the observed transient pressure-denatured states have characteristics of molten globules.
authors.affiliation: Centre de Recherches du Service de Santé des Armées, Unité de Biochemie, La Tronche, France.
authors.forename: C
authors.initials: C
authors.lastname: Cléry
authors.forename: F
authors.initials: F
authors.lastname: Renault
authors.forename: P
authors.initials: P
authors.lastname: Masson
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000737:chemistry / Q000378:metabolism; D002091:Butyrylcholinesterase / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005453:Fluorescence; D006801:Humans; D011312:Pressure; D017510:Protein Folding; D012044:Regression Analysis
chemical_list: D000817:Anilino Naphthalenesulfonates; D002091:Butyrylcholinesterase