Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita, Yoshikatsu Aikawa

Research output: Contribution to journalArticle

8 Citations (Scopus)

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).

Original languageEnglish
Pages (from-to)467-470
Number of pages4
JournalJournal of biochemistry
Volume117
Issue number3
DOIs
Publication statusPublished - Jan 1 1995
Externally publishedYes

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Multienzyme Complexes
Pyruvate Dehydrogenase Complex
Geobacillus stearothermophilus
Bacilli
Pyruvic Acid
Gel Chromatography
Oxidoreductases
Gels
Column chromatography
Ultracentrifugation
Dynamic light scattering
Chromatography
Sepharose
Sucrose
Proteins
Dynamic Light Scattering

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. / Hiromasa, Yasuaki; Aso, Yoichi; Yamashita, Shoji; Aikawa, Yoshikatsu.

In: Journal of biochemistry, Vol. 117, No. 3, 01.01.1995, p. 467-470.

Research output: Contribution to journalArticle

Hiromasa, Yasuaki ; Aso, Yoichi ; Yamashita, Shoji ; Aikawa, Yoshikatsu. / Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. In: Journal of biochemistry. 1995 ; Vol. 117, No. 3. pp. 467-470.
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