In the course of protein-structure determinations of the membrane-bound enzyme monoamine oxidase B (MAO B) by X-ray crystallography, a compound was found in the active site of the enzyme that consists of two phenyl rings separated by four C atoms. This compound was identified by chromatography and by mass spectrometry to be 1,4-diphenyl-2-butene and found to be a component of the polystyrene microbridges that are used in protein crystallization. This compound is present at a level of approximately 0.3 mg ( approximately 1.5 micro mol) per microbridge and functions as a competitive inhibitor of MAO B with a K(i) of 35 micro M. The presence of detergents in the crystallization solutions facilitates the extraction of this compound from the polymer medium.

Polystyrene microbridges used in sitting-drop crystallisation release 1,4-diphenyl-2-butene, a novel inhibitor of human MAO B

BINDA, CLAUDIA;MATTEVI, ANDREA;
2003-01-01

Abstract

In the course of protein-structure determinations of the membrane-bound enzyme monoamine oxidase B (MAO B) by X-ray crystallography, a compound was found in the active site of the enzyme that consists of two phenyl rings separated by four C atoms. This compound was identified by chromatography and by mass spectrometry to be 1,4-diphenyl-2-butene and found to be a component of the polystyrene microbridges that are used in protein crystallization. This compound is present at a level of approximately 0.3 mg ( approximately 1.5 micro mol) per microbridge and functions as a competitive inhibitor of MAO B with a K(i) of 35 micro M. The presence of detergents in the crystallization solutions facilitates the extraction of this compound from the polymer medium.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/113210
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