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).
Hiromasa
Y
Y
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka.
Aso
Y
Y
Yamashita
S
S
Aikawa
Y
Y
D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D008027:Light; D011768:Pyruvate Dehydrogenase Complex / Q000032:analysis*; D012542:Scattering, Radiation; D014461:Ultracentrifugation
D011768:Pyruvate Dehydrogenase Complex