Hiromasa Y, Aso Y, Yamashita S, Aikawa Y
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka.
J Biochem. 1995 Mar;117(3):467-70. doi: 10.1093/oxfordjournals.jbchem.a124730.
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).
通过六次凝胶过滤柱色谱法从嗜热脂肪芽孢杆菌中纯化丙酮酸脱氢酶多酶复合物；一次使用Cellulofine GCL - 2000，两次使用琼脂糖凝胶CL - 2B，三次使用Sephacryl S - 500HR。通过凝胶过滤色谱法、分析型和蔗糖密度超速离心法以及动态光散射详细研究了该复合物的分子大小分布。发现该复合物是均一的；即使在高浓度蛋白质（低于6.8 mg/ml）下也未检测到二聚体复合物。
