Escherichia coli flavodoxin sepharose as an affinity resin for cytochromes P450 and use to identify a putative cytochrome P450c17/3beta-hydroxysteroid dehydrogenase interaction.

Jenkins, C M

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

Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.

0003-9861

10.1006/abbi.1997.0318 doi


3-Hydroxysteroid Dehydrogenases--metabolism
Adrenal Cortex--enzymology
Animals
Cattle
Chromatography, Affinity--methods
Cloning, Molecular
Cytochrome P-450 Enzyme System--isolation & purification
Electrophoresis, Polyacrylamide Gel
Escherichia coli--genetics
Flavodoxin--analogs & derivatives
Immunoblotting
Peptide Fragments--analysis
Protein Binding
Recombinant Proteins--metabolism
Sepharose--analogs & derivatives
Steroid 17-alpha-Hydroxylase--genetics
Steroid 21-Hydroxylase
Steroids--biosynthesis