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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus.

The pyruvate dehydrogenase multienzyme complex was purified from Bacillus stearothermophilus by means of six gel-filtration column chromatographies; once on Cellulofine GCL-2000, twice on Sepharose CL-2B, and three times on Sephacryl S-500HR. The molecular size distribution of the complex was examined in detail by gel-filtration chromatography, analytical and sucrose-density ultracentrifugations, and dynamic light scattering. The complex was found to be homogeneous; a dimeric complex was undetectable even with a high concentration of protein (below 6.8 mg/ml).[1]


  1. Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. Hiromasa, Y., Aso, Y., Yamashita, S., Aikawa, Y. J. Biochem. (1995) [Pubmed]
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