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Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus
Y Hiromasa1, Y Aso, S Yamashita
1Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka.
Journal of Biochemistry
|March 1, 1995
Abstract:
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).