PRESSURE-INDUCED MOLTEN GLOBULE STATE OF CHOLINESTERASE

The denaturing effect of pressure on the structure of human butyrylcho linesterase 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 t hat pressure denaturation of butyrylcholinesterase is a multi-step pro cess and that the observed transient pressure-denatured states have ch aracteristics of molten globules.