Purification and characterization of a soluble form of rat liver NADPH-cytochrome P-450 reductase highly expressed in Escherichia coli

2003 ◽  
Vol 29 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Shunsuke Hayashi ◽  
Yoshiaki Omata ◽  
Hiroshi Sakamoto ◽  
Takayuki Hara ◽  
Masato Noguchi
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Soluble Form ◽  
Purification And Characterization ◽  
Nadph Cytochrome ◽  
Cytochrome P 450

Purification and characterization of NADPH-cytochrome P-450 reductase from rat epidermis

1993 ◽  
Vol 53 (3) ◽  
pp. 206-212 ◽  
Author(s):  
Hidenari Takahara ◽  
Syed I. A. Zaidi ◽  
Hasan Mukhtar ◽  
Masafumi Handa ◽  
William L. Epstein ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Nadph Cytochrome ◽  
Cytochrome P 450

Purification and characterization of D-β-hydroxybutyrate dehydrogenase expressed in Escherichia coli

1993 ◽  
Vol 71 (7-8) ◽  
pp. 406-410
Author(s):  
Les Jones ◽  
Sharon Churchill ◽  
Perry Churchill
Keyword(s):  
Escherichia Coli ◽  
Kinetic Parameters ◽  
Functional Properties ◽  
Rat Liver ◽  
Specific Activity ◽  
Purification And Characterization ◽  
E Coli ◽  
Specific Activities ◽  
Viable Method

D-β-Hydroxybutyrate dehydrogenase (BDH), a lipid-requiring enzyme, has been cloned into pUC18, expressed in Escherichia coli, and purified to homogeneity. The apoenzyme, i.e., the enzyme devoid of phospholipid, has no activity, but can be activated by phospholipid to a specific activity of 129 μmol/(min∙mg). The functional properties of the enzyme expressed in E. coli were compared with the enzyme purified from rat liver. The specific activities, kinetic parameters, and phospholipid activation profiles were virtually identical. These results indicate that the expression of the enzyme in E. coli is a viable method for producing active functional BDH and should allow for the production of specifically altered BDH molecules.Key words: D-β-hydroxybutyrate dehydrogenase, cloning, expression, lipid requiring.

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