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Resistance Mechanism of Chloramphenicol in Streptococcus haemolyticus, Streptococcus pneumoniae and Streptococcus faecalis
Author(s) -
Miyamura Sadao,
Ochiai Hiroshi,
Nitahara Yoshiyuki,
Nakagawa Yoji,
Terao Michinori
Publication year - 1977
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1977.tb02809.x
Subject(s) - ammonium sulfate precipitation , streptococcus pneumoniae , microbiology and biotechnology , chloramphenicol , staphylococcus haemolyticus , streptococcus , sephadex , biology , streptococcus suis , streptococcus bovis , bacteria , enzyme , size exclusion chromatography , chromatography , biochemistry , chemistry , fermentation , antibiotics , staphylococcus , staphylococcus aureus , rumen , genetics , virulence , gene
The chloramphenicol resistance of Streptococcus haemolyticus, Streptococcus pneumoniae and Streptococcus faecalis isolated from clinical materials was proved to be due to an inactivating enzyme produced by these bacteria. The inactivated products of chloramphenicol were identified as 1‐acetoxy, 3‐acetoxy and 1,3‐diacetoxy derivatives by thin‐layer chromatography and infrared spectroscopy. The responsible enzyme was thus confirmed to be chloramphenicol acetyltransferase. The enzyme was inducible. It was partially purified by ammonium sulfate precipitation, DEAE‐cellulose chromatography and gel filtration on Sephadex G‐150. The enzymes obtained from S. haemolyticus, S. pneumoniae and S. faecalis have been compared with the conclusion that they are identical with respect to molecular weight (approximately 75,000–80,000), optimum pH and heat stability.