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Journal Article

An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schubert, D., Maurer, E., Boss, K., & Pfleiderer, G. (1984). An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium. Hoppe-Seyler's Zeitschrift für physiologische Chemie, 365(12), 1445-1449. doi:10.1515/bchm2.1984.365.2.1445.


Cite as: https://hdl.handle.net/21.11116/0000-0008-CD53-4
Abstract
The self-association of glucose dehydrogenase (beta-D-glucose:NAD(P) 1-oxidoreductase, EC 1.1.1.47) from Bacillus megaterium was studied by analytical ultracentrifugation. The pH and composition of the buffer used were such that, owing to a reversible partial dissociation of the tetrameric enzyme, enzyme activity was reduced. It was found that under these conditions the protein exists in a monomer/dimer/tetramer association equilibrium.