The application of triazine dye affinity chromatography to the large-scale purification of glycerokinase from Bacillus stearothermophilus.
Anal Biochem
; 132(2): 413-7, 1983 Jul 15.
Article
em En
| MEDLINE
| ID: mdl-6312842
ABSTRACT
Gram quantities of homogeneous glycerokinase have been prepared from the thermophilic bacterium, Bacillus stearothermophilus, using three major steps:
precipitation of debris at pH 5.1, ion-exchange chromatography on DEAE-Sephadex, and affinity chromatography on Procion Blue MX-3G-Sepharose. This method is a considerable improvement over conventional techniques; the purified enzyme was obtained with a 40% recovery and a specific activity of 120 units (mumol/min)/mg protein. A modified culture medium enabled yields of 3.4 X 10(6) units of enzyme to be obtained from 400-liter production cultures.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfotransferases
/
Geobacillus stearothermophilus
/
Glicerol Quinase
Idioma:
En
Revista:
Anal Biochem
Ano de publicação:
1983
Tipo de documento:
Article