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Pressure‐induced molten globule state of cholinesterase
Author(s) -
Cléry C.,
Renault F.,
Masson P.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00787-a
Subject(s) - molten globule , cholinesterase , chemistry , biophysics , thermodynamics , materials science , biochemistry , medicine , biology , physics , protein structure
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.