Jenkins, C M <br/><br/>
Escherichia coli flavodoxin sepharose as an affinity resin for cytochromes P450 and use to identify a putative cytochrome P450c17/3beta-hydroxysteroid dehydrogenase interaction.  [electronic resource] 

 -  Archives of biochemistry and biophysics  Nov 1997 
 - 93-102 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0003-9861 
<br/><br/><label>Standard No.: </label>10.1006/abbi.1997.0318  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>3-Hydroxysteroid Dehydrogenases--metabolism<br/>Adrenal Cortex--enzymology<br/>Animals<br/>Cattle<br/>Chromatography, Affinity--methods<br/>Cloning, Molecular<br/>Cytochrome P-450 Enzyme System--isolation & purification<br/>Electrophoresis, Polyacrylamide Gel<br/>Escherichia coli--genetics<br/>Flavodoxin--analogs & derivatives<br/>Immunoblotting<br/>Peptide Fragments--analysis<br/>Protein Binding<br/>Recombinant Proteins--metabolism<br/>Sepharose--analogs & derivatives<br/>Steroid 17-alpha-Hydroxylase--genetics<br/>Steroid 21-Hydroxylase<br/>Steroids--biosynthesis