Enzymatic studies on the mechanism of action of cefoxitin. Correlation between the affinities of cefoxitin to penicillin-binding proteins and its rates of inhibition of the respective penicillin-sensitive reactions in E. coli
| Autor: | Shigeo Tamaki, Michio Matsuhashi |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Penicillin binding proteins
Penicillins medicine.disease_cause Binding Competitive Cefoxitin Bacterial Proteins Drug Discovery Escherichia coli polycyclic compounds medicine Pharmacology chemistry.chemical_classification Chemistry Penicillin G Affinities Cephalosporins Penicillin Enzyme Biochemistry Mechanism of action medicine.symptom Carrier Proteins Cephamycin Protein Binding medicine.drug |
| Zdroj: | The Journal of Antibiotics. 31:1292-1295 |
| ISSN: | 1881-1469 0021-8820 |
| DOI: | 10.7164/antibiotics.31.1292 |
| Popis: | The affinities of cefoxitin, a cephamycin antibiotic, to penicillin-binding proteins of Escherichia coli were reexamined using a recently developed method for separating penicillin-binding proteins. The inhibitions by this antibiotic of four measurable penicillin-sensitive enzymatic reactions, the reactions of D-alanine carboxypeptidases IA and IB, cross-bridge formation and concomitant release of D-alanine, were also measured. An approximate correlation was found between the affinities of cefoxitin to the penicillin-binding proteins responsible for these reactions and its rates of inhibition of the respective penicillin-sensitive reactions. |
| Databáze: | OpenAIRE |
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