Jenkins, C M <br/><br/>
Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities.  [electronic resource] 

 -  The Journal of biological chemistry  Nov 1994 
 - 27401-8 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Aldehyde-Lyases--metabolism<br/>Amino Acid Sequence<br/>Animals<br/>Bacterial Proteins--metabolism<br/>Cattle<br/>Cytochrome P-450 Enzyme System--metabolism<br/>Enzyme Activation<br/>Escherichia coli--metabolism<br/>Ferredoxin-NADP Reductase--metabolism<br/>Flavodoxin--metabolism<br/>Molecular Sequence Data<br/>NAD--metabolism<br/>NADH, NADPH Oxidoreductases--metabolism<br/>NADPH-Ferrihemoprotein Reductase--chemistry<br/>Progesterone--metabolism<br/>Rats<br/>Recombinant Proteins<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Spectrum Analysis<br/>Steroid 17-alpha-Hydroxylase