Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli

Biochemical and Biophysical Research Communications

Volumn 344, Issue 1, 2006, Pages 400-405

  Arase, Miharu ^a   Waterman, Michael R ^a   Kagawa, Norio ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Congenital adrenal hyperplasia; CYP21; Escherichia coli expression; Molecular chaperone; Steroid hormone

Indexed keywords

CHAPERONE; CHAPERONIN; CHOLIC ACID; CYTOCHROME P450; HYDROXYPROGESTERONE; MONOMER; PROGESTERONE; STEROID 21 MONOOXYGENASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM CULTURE; BINDING ASSAY; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; COW; ENZYME ANALYSIS; ENZYME ENGINEERING; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GEL FILTRATION; GENE EXPRESSION SYSTEM; MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONTENT; PROTEIN EXPRESSION; SOLUBILITY;

17-ALPHA-HYDROXYPROGESTERONE; ANIMALS; CATTLE; CYTOCHROME P-450 ENZYME SYSTEM; ESCHERICHIA COLI; GENETIC ENGINEERING; PROGESTERONE; RECOMBINANT PROTEINS; SOLUBILITY; STEROID 21-HYDROXYLASE;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI;

EID: 33646030623     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.067     Document Type: Article

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