Molecular characterization of the Acremonium chrysogenum cefG gene product: The native deacetylcephalosporin C acetyltransferase is not processed into subunits

Biochemical Journal

Volumn 337, Issue 3, 1999, Pages 379-385

  Velasco, Javier ^a   Gutierrez, Santiago ^a   Campoy, Sonia ^a   Martin, Juan F ^a  

^a UNIVERSITY OF LEÓN   (Spain)

Author keywords

Cephalosporin C; Immunodetection; Protein processing

Indexed keywords

ACYLTRANSFERASE; CEPHALOSPORIN C; DEACETYLCEPHALOSPORIN C; GENE PRODUCT; METHIONINE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CEPHALOSPORIUM ACREMONIUM; CODON; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE CONSTRUCT; GENE EXPRESSION; IMMUNOAFFINITY CHROMATOGRAPHY; IMMUNOBLOTTING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION;

ACETYLTRANSFERASES; ACREMONIUM; AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CEPHALOSPORINS; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; FUNGAL PROTEINS; MOLECULAR WEIGHT; MUTATION; RABBITS; SOLUBILITY;

ACREMONIUM CHRYSOGENUM; CEPHALOSPORIUM; ESCHERICHIA COLI;

EID: 0033083406     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3370379     Document Type: Article

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