Purification and properties of a shortened form of cytochrome P-450 2E1: Deletion of the NH2-terminal membrane-insertion signal peptide does not alter the catalytic activities

Proceedings of the National Academy of Sciences of the United States of America

Volumn 88, Issue 20, 1991, Pages 9141-9145

  Larson, Jane R ^a   Coon, Minor J ^a   Porter, Todd D ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b University of Kentucky   (United States)

Author keywords

Alcohol oxidation; Alcohol inducible P 450; Heterologous expression in escherichia coli; Membrane binding; Rabbit liver microsomal cytochrome P 450

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

CYTOCHROME P450;

ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION; LIVER MICROSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; RABBIT; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; CHROMATOGRAPHY; CHROMATOGRAPHY, ION EXCHANGE; CHROMOSOME DELETION; COMPARATIVE STUDY; CYTOCHROME P-450 CYP2E1; CYTOCHROME P-450 ENZYME SYSTEM; DURAPATITE; HYDROXYAPATITES; KINETICS; MOLECULAR SEQUENCE DATA; NADPH-FERRIHEMOPROTEIN REDUCTASE; OXIDOREDUCTASES, N-DEMETHYLATING; PROTEIN SORTING SIGNALS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0026046620     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.88.20.9141     Document Type: Article

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