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[Identification of the beta lactamase R-TEM of Pseudomonas aeruginosa].
- Source :
-
Biochimie [Biochimie] 1975; Vol. 57 (2), pp. 139-43. - Publication Year :
- 1975
-
Abstract
- This paper is dealing with the enzymatic problem raised by two strains of Ps. aeruginosa resistant to classical beta lactam antibiotics including carbenicillin. These two strains hydrolyse all these antibiotics. In both cases, we have shown the simultaneous biosynthesis of two enzymes: an inducible and chromosome cephalosporinase frequently found in this germ, and a constitutive beta lactamase, with a penicillinase activity which has been identified with the extrachromosomic beta lactamase R-TEM. These two enzymes have been separated by affinity chromatography, characterized by their kinetic constants given by computerized microacidimetry, and their isoelectric points which are respectively 9.2 for the cephalosporinase and 5.40 for the penicillinase R-TEM. Isoelectric focussing also shows the separation of these two enzymes.
- Subjects :
- Ampicillin metabolism
Carbenicillin metabolism
Cephalexin metabolism
Cephaloridine metabolism
Cephalosporinase metabolism
Cephalothin metabolism
Chromatography, Affinity
Isoelectric Focusing
Kinetics
Penicillin G metabolism
Penicillin Resistance
Penicillin V metabolism
Penicillinase metabolism
Structure-Activity Relationship
Amidohydrolases isolation & purification
Cephalosporinase isolation & purification
Penicillinase isolation & purification
Pseudomonas aeruginosa enzymology
Subjects
Details
- Language :
- French
- ISSN :
- 0300-9084
- Volume :
- 57
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochimie
- Publication Type :
- Academic Journal
- Accession number :
- 806305
- Full Text :
- https://doi.org/10.1016/s0300-9084(75)80163-5