Rapid testing of susceptibility of Haemophilus influenzae to chloramphenicol by a bioluminescence method. 1990

C H Park, and D L Hixon, and L M Berger

UI MeSH Term Description Entries
D002701 Chloramphenicol An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106) Cloranfenicol,Kloramfenikol,Levomycetin,Amphenicol,Amphenicols,Chlornitromycin,Chlorocid,Chloromycetin,Detreomycin,Ophthochlor,Syntomycin
D002702 Chloramphenicol Resistance Nonsusceptibility of bacteria to the action of CHLORAMPHENICOL, a potent inhibitor of protein synthesis in the 50S ribosomal subunit where amino acids are added to nascent bacterial polypeptides. Chloramphenicol Resistances
D006193 Haemophilus influenzae A species of HAEMOPHILUS found on the mucous membranes of humans and a variety of animals. The species is further divided into biotypes I through VIII. Bacterium influenzae,Coccobacillus pfeifferi,Haemophilus meningitidis,Hemophilus influenzae,Influenza-bacillus,Mycobacterium influenzae
D001431 Bacteriological Techniques Techniques used in studying bacteria. Bacteriologic Technic,Bacteriologic Technics,Bacteriologic Techniques,Bacteriological Technique,Technic, Bacteriological,Technics, Bacteriological,Technique, Bacteriological,Techniques, Bacteriological,Bacteriologic Technique,Bacteriological Technic,Bacteriological Technics,Technic, Bacteriologic,Technics, Bacteriologic,Technique, Bacteriologic,Techniques, Bacteriologic
D015500 Chloramphenicol O-Acetyltransferase An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28. CAT Enzyme,Chloramphenicol Acetyltransferase,Chloramphenicol Transacetylase,Acetyltransferase, Chloramphenicol,Chloramphenicol O Acetyltransferase,Enzyme, CAT,O-Acetyltransferase, Chloramphenicol,Transacetylase, Chloramphenicol

Related Publications

C H Park, and D L Hixon, and L M Berger
December 1987, Journal of clinical microbiology,
C H Park, and D L Hixon, and L M Berger
April 1987, The Pediatric infectious disease journal,
C H Park, and D L Hixon, and L M Berger
January 1977, American journal of clinical pathology,
C H Park, and D L Hixon, and L M Berger
February 1986, Diagnostic microbiology and infectious disease,
C H Park, and D L Hixon, and L M Berger
November 1982, Journal of clinical microbiology,
C H Park, and D L Hixon, and L M Berger
April 2000, The Journal of antimicrobial chemotherapy,
C H Park, and D L Hixon, and L M Berger
December 1978, Immunitat und Infektion,
C H Park, and D L Hixon, and L M Berger
May 1987, Antimicrobial agents and chemotherapy,
C H Park, and D L Hixon, and L M Berger
January 1977, Lancet (London, England),
Copied contents to your clipboard!