Acetate kinase (EC 2.7.2.1), an enzyme involved in the wasteful production of acetate during conversion of cellulose to ethanol by Clostridlum thermocellum, was purified 144-fold. The enzyme has an Mr of 84 kD by non-denaturing gradient gel electrophoresis, and an Mr of 46 kD when estimated with a d
β¦ LIBER β¦
Purification and immobilization of acetate kinase from Desulfovibrio vulgaris
β Scribed by Geert Mannens; Guido Slegers; Albert Claeys
- Publisher
- Springer Netherlands
- Year
- 1988
- Tongue
- English
- Weight
- 406 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0141-5492
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Purification and characterization of ace
β
Wenglong R. Lin; Yulin Peng; Scott Lew; Claudia C. Lee; Janet J. Hsu; Jean-Franc
π
Article
π
1998
π
Elsevier Science
π
French
β 434 KB
292 - Electrode reaction of cytochrome c
β
P. Bianco; G. Fauque; J. Haladjian
π
Article
π
1979
π
Elsevier Science
π
English
β 447 KB
Purification and properties of acetate k
β
Annabella Schaupp; Lars G. Ljungdahl
π
Article
π
1974
π
Springer
π
English
β 526 KB
Acetate kinase (ATP: acetate phosphotransferase E C 2.7.2.1) has been purified from Clostrldium thermoaceticum. The enzyme of a specific activity of 282 ~moles rain -1 nag -1 appeared homogeneous as judged from Sephadex chromate. graphy and sedimentation velocity. Polyacrytamide gel electrophoretic
Immobilization of acetate kinase and pho
β
G. Mannens; G. Slegers; R. Lambrecht; H. De Langhe; K. Puttemans; C. Block
π
Article
π
1987
π
Elsevier Science
π
English
β 459 KB
Spectroscopic and redox properties of ad
β
M.F.J.M. Verhagen; I. Kooter; R.B.G. Wolbert; W.R. Hagen
π
Article
π
1993
π
Elsevier Science
π
English
β 74 KB
Molecular properties of the dissimilator
β
J. Steube; A.F. Arendsen; W.R. Hagen; P.M.H. Kroneck
π
Article
π
1994
π
Elsevier Science
π
English
β 70 KB