Biomaterial Database

[Isolation and purification of the chloramphenicol-acetyltransferase from Y. pestis EV cells with extrachromosomal resistance to the antibiotic by affinity chromatography]. 1981

N V Korobeĭnik, and B N Mishan'kin

Purification of chloramphenicol acetyltransferase isolated from the cells of Y. pestis EV-R with extrachromosomal resistance to chloramphenicol included ultrafiltration on the microporous membranes Diaflo-XM 300 and biospecific chromatography on columns with cepharose 4B covalently bound with the reduced chloramphenicol. Elution of chloramphenicol acetyltransferase was achieved by means of addition of native chloramphenicol to the buffer solution. Such native chloramphenicol had higher affinity to the enzyme than the reduced antibiotic. As a result the enzyme preparations with 250 times higher purity levels and 70 per cent of the initial activity were obtained. The disc electrophoresis of the sample in polyacrylamide gel produced a single protein zone capable of chloramphenicol acetylation in the presence of Ac approximately CoA.

UI	MeSH Term	Description	Entries
D011815	R Factors	A class of plasmids that transfer antibiotic resistance from one bacterium to another by conjugation.	R Factor,R Plasmid,R Plasmids,Resistance Factor,Resistance Factors,Factor, R,Factor, Resistance,Factors, R,Factors, Resistance,Plasmid, R,Plasmids, R
D002846	Chromatography, Affinity	A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D004352	Drug Resistance, Microbial	The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS).	Antibiotic Resistance,Antibiotic Resistance, Microbial,Antimicrobial Resistance, Drug,Antimicrobial Drug Resistance,Antimicrobial Drug Resistances,Antimicrobial Resistances, Drug,Drug Antimicrobial Resistance,Drug Antimicrobial Resistances,Drug Resistances, Microbial,Resistance, Antibiotic,Resistance, Drug Antimicrobial,Resistances, Drug Antimicrobial
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005111	Extrachromosomal Inheritance	Vertical transmission of hereditary characters by DNA from cytoplasmic organelles such as MITOCHONDRIA; CHLOROPLASTS; and PLASTIDS, or from PLASMIDS or viral episomal DNA.	Cytoplasmic Inheritance,Extranuclear Inheritance,Inheritance, Cytoplasmic,Inheritance, Extrachromosomal,Inheritance, Extranuclear
D000123	Acetyltransferases	Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.	Acetyltransferase
D015010	Yersinia pestis	The etiologic agent of PLAGUE in man, rats, ground squirrels, and other rodents.	Bacillus pestis,Bacterium pestis,Pasteurella pestis,Pestisella pestis,Yersinia pseudotuberculosis subsp. pestis
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