Cytochrome P450 4A4: Expression in Escherichia coli, purification, and characterization of catalytic properties

Biochemistry ◽  
1993 ◽  
Vol 32 (34) ◽  
pp. 8863-8870 ◽  
Author(s):  
Masazumi Nishimoto ◽  
Joan E. Clark ◽  
Bettie Sue Siler Masters
Keyword(s):  
Escherichia Coli ◽  
Cytochrome P450 ◽  
Catalytic Properties ◽  
Purification And Characterization ◽  
Expression In Escherichia Coli

scholarly journals Purification and characterization of 3-dehydroquinase from Escherichia coli

1986 ◽  
Vol 239 (3) ◽  
pp. 699-704 ◽  
Author(s):  
S Chaudhuri ◽  
J M Lambert ◽  
L A McColl ◽  
J R Coggins
Keyword(s):  
Escherichia Coli ◽  
Gel Electrophoresis ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Permeation Chromatography ◽  
Purification And Characterization ◽  
Gel Permeation

A procedure has been developed for the purification of 3-dehydroquinase from Escherichia coli. Homogeneous enzyme with specific activity 163 units/mg of protein was obtained in 19% overall yield. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 29,000. The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric. The catalytic properties of the enzyme have been determined and shown to be very similar to those of the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of Neurospora crassa.

High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2

2003 ◽  
Vol 31 (2) ◽  
pp. 250-259 ◽  
Author(s):  
Katrin Lehmann ◽  
Silke Hoffmann ◽  
Philipp Neudecker ◽  
Martin Suhr ◽  
Wolf-Meinhard Becker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Yield ◽  
Purification And Characterization ◽  
Peanut Allergen ◽  
Ara H 2 ◽  
Expression In Escherichia Coli
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