Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita, Yoshikatsu Aikawa

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8 Citations (Scopus)


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).

Original languageEnglish
Pages (from-to)467-470
Number of pages4
JournalJournal of biochemistry
Issue number3
Publication statusPublished - Mar 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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