Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus.
J Biochem
; 117(3): 467-70, 1995 Mar.
Article
em En
| MEDLINE
| ID: mdl-7629008
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).
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Base de dados:
MEDLINE
Assunto principal:
Complexo Piruvato Desidrogenase
/
Geobacillus stearothermophilus
Idioma:
En
Revista:
J Biochem
Ano de publicação:
1995
Tipo de documento:
Article