PMID: 8954151Nov 15, 1996Paper

Monoamine oxidase B isolated from bovine liver exists as large oligomeric complexes in vitro

European Journal of Biochemistry
B A ShiloffC W Abell

Abstract

The quaternary structure and subunit composition of bovine liver monoamine oxidase B (MAO B) was investigated using size-exclusion chromatography, sucrose gradient centrifugation and electron microscopy. Purified enzyme was subjected to Superdex gel filtration column chromatography in the presence of the non-ionic detergents, n-octyl beta-D-glucopyranoside (octyl glucoside) and Triton X-100R-PC (Triton). The specific activity and elution profiles indicate that the enzyme exists as a dimer and preferentially functions as larger oligomeric complexes. Distribution of the oligomeric forms of MAO B was found to be dependent upon protein concentration. Dilution of the enzyme, however, had little or no effect upon the specific activity profiles. In Triton and octyl glucoside, plots of specific activity versus molecular mass displayed a sigmoidal shape. The chromatographic data suggest that detergent-solubilized bovine liver MAO B exists as cooperative oligomeric enzyme complexes. Similarly, sucrose density gradient centrifugation of purified MAO B exhibited a direct correlation between enzyme activity and molecular mass of the MAO complexes. MAO B activity was found to be widely distributed throughout the sucrose gradient and the high...Continue Reading

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Apr 3, 2012·Journal of Physiology and Biochemistry·Nadia Z ShabanOmayma M Sadek
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May 22, 2009·Biochemistry·Rossen ApostolovHaruki Nakamura

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