Kinetics of antimicrobial activity of aztreonam/clavulanic acid (2:1) against Xanthomonas maltophilia

1991 ◽  
Vol 27 (4) ◽  
pp. 552-554 ◽  
Author(s):  
J. A. GARCÍA-RODRÍGUEZ ◽  
J. E. GARCÍA SÁNCHEZ ◽  
J. L. MUÑOZ BELLIDO ◽  
M. I. GARCÍA GARCÍA ◽  
E. GARCÍA SANCHEZ
Keyword(s):  
Antimicrobial Activity ◽  
Clavulanic Acid ◽  
Xanthomonas Maltophilia ◽  
Kinetics Of

Kinetics of Antimicrobial Activity of Amoxicillin/Clavulanic Acid and Metronidazole against β-Lactamase-ProducingBacteroides fragilisGroup

1990 ◽  
Vol 2 (1) ◽  
pp. 11-16 ◽  
Author(s):  
J.A. García-Rodríguez ◽  
J.E. García Sánchez ◽  
I. Trujillano ◽  
J.L. Muñoz - Bellido
Keyword(s):  
Antimicrobial Activity ◽  
Clavulanic Acid ◽  
Amoxicillin Clavulanic Acid ◽  
Kinetics Of

scholarly journals Antimicrobial activity and time kill kinetics of Nigerian Honeys on multi-resistant Enteric Bacilli

2018 ◽  
Vol 210 ◽  
pp. 012003
Author(s):  
P.A Akinduti ◽  
A Oluwadun ◽  
J.A.O Olugbuyiro ◽  
C.S Osuagwu ◽  
O Ejilude ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Time Kill ◽  
Kinetics Of

scholarly journals Sequence analysis and enzyme kinetics of the L2 serine beta-lactamase from Stenotrophomonas maltophilia.

1997 ◽  
Vol 41 (7) ◽  
pp. 1460-1464 ◽  
Author(s):  
T R Walsh ◽  
A P MacGowan ◽  
P M Bennett
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Clavulanic Acid ◽  
Active Site ◽  
Stenotrophomonas Maltophilia ◽  
Leader Peptide ◽  
Beta Lactamase ◽  
Class A ◽  
Cloned Gene ◽  
Kinetics Of

The L2 serine active-site beta-lactamase from Stenotrophomonas maltophilia has been classified as a clavulanic acid-sensitive cephalosporinase. The gene encoding this enzyme from S. maltophilia 1275 IID has been cloned on a 3.3-kb fragment into pK18 under the control of a Ptac promoter to generate recombinant plasmid pUB5840; when expressed in Escherichia coli, this gene confers resistance to cephalosporins and penicillins. Sequence analysis has revealed an open reading frame (ORF) of 909 bp with a GC content of 71.6%, comparable to that of the L1 metallo-beta-lactamase gene (68.4%) from the same bacterium. The ORF encodes an unmodified protein of 303 amino acids with a predicted molecular mass of 31.5 kDa, accommodating a putative leader peptide of 27 amino acids. Comparison of the amino acid sequence with those of other beta-lactamases showed it to be most closely related (54% identity) to the BLA-A beta-lactamase from Yersinia enterocolitica. Sequence identity is most obvious near the STXK active-site motif and the SDN loop motif common to all serine active-site penicillinases. Sequences outside the conserved regions display low homology with comparable regions of other class A penicillinases. Kinetics of the enzyme from the cloned gene demonstrated an increase in activity with cefotaxime but markedly less activity with imipenem than previously reported. Hence, the S. maltophilia L2 beta-lactamase is an inducible Ambler class A beta-lactamase which would account for the sensitivity to clavulanic acid.

scholarly journals Burkholderia pseudomallei Class A β-Lactamase Mutations That Confer Selective Resistance against Ceftazidime or Clavulanic Acid Inhibition

2003 ◽  
Vol 47 (7) ◽  
pp. 2082-2087 ◽  
Author(s):  
Chanwit Tribuddharat ◽  
Richard A. Moore ◽  
Patricia Baker ◽  
Donald E. Woods
Keyword(s):  
Sequence Analysis ◽  
Enzyme Kinetics ◽  
Clavulanic Acid ◽  
Burkholderia Pseudomallei ◽  
Acid Inhibition ◽  
Regulator Gene ◽  
Class A ◽  
Resistance Patterns ◽  
Kinetics Of ◽  
Lactamase Inhibitor

ABSTRACT Burkholderia pseudomallei, the causative agent of melioidosis, is inherently resistant to a variety of antibiotics including aminoglycosides, macrolides, polymyxins, and β-lactam antibiotics. Despite resistance to many β-lactams, ceftazidime and β-lactamase inhibitor-β-lactam combinations are commonly used for treatment of melioidosis. Here, we examine the enzyme kinetics of β-lactamase isolated from mutants resistant to ceftazidime and clavulanic acid inhibition and describe specific mutations within conserved motifs of the β-lactamase enzyme which account for these resistance patterns. Sequence analysis of regions flanking the B. pseudomallei penA gene revealed a putative regulator gene located downstream of penA. We have cloned and sequenced the penA gene from B. mallei and found it to be identical to penA from B. pseudomallei.

scholarly journals Synthesis and Characterization of Gellan Gum-Pyridoxine Nanoparticle for Treatment of Localized Peripheral Neuropathy

2019 ◽  
Vol 9 (1S4) ◽  
pp. 576-580
Keyword(s):  
Antimicrobial Activity ◽  
Peripheral Neuropathy ◽  
Release Kinetics ◽  
Drug Carrier ◽  
Gellan Gum ◽  
Synthesis And Characterization ◽  
Antioxidant Assay ◽  
Gram Positive Bacteria ◽  
Kinetics Of

Biopolymer has full application as a drug carrier and scaffold in tissue engineering because of its biodegradability and non-toxicity. The present study is focused on novel biopolymer gellan gum as a drug delivery agent. The objective of the study is to synthesize the gellan gum nanoparticle by solvent evaporation emulsification method and characterize it using SEM, DLS, FTIR, and XRD. As pyridoxine is effectively used to treat diabetic peripheral neuropathy, it has been encapsulated with gellan gum and characterized. The antioxidant assay was performed using ABTS reagent, and the activity increases with increasing concentration of nanoparticle. Also, it has significant antimicrobial activity against gram-positive bacteria. Apart from this, the drug release kinetics of the gellan gum- pyridoxine nanoparticle was studied.

scholarly journals Degradation Kinetics of Clavulanic Acid in Fermentation Broths at Low Temperatures

Antibiotics ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 6 ◽  
Author(s):  
David Gómez-Ríos ◽  
Howard Ramírez-Malule ◽  
Peter Neubauer ◽  
Stefan Junne ◽  
Rigoberto Ríos-Estepa
Keyword(s):  
Kinetic Model ◽  
Clavulanic Acid ◽  
Low Temperatures ◽  
High Performance ◽  
Degradation Kinetics ◽  
Streptomyces Clavuligerus ◽  
Submerged Cultures ◽  
Fast Decline ◽  
Fermentation Broths ◽  
Kinetics Of

Clavulanic acid (CA) is a β-lactam antibiotic inhibitor of β-lactamase enzymes, which confers resistance to bacteria against several antibiotics. CA is produced in submerged cultures by the filamentous Gram-positive bacterium Streptomyces clavuligerus; yield and downstream process are compromised by a degradation phenomenon, which is not yet completely elucidated. In this contribution, a study of degradation kinetics of CA at low temperatures (−80, −20, 4, and 25 °C) and pH 6.8 in chemically-defined fermentation broths is presented. Samples of CA in the fermentation broths showed a fast decline of concentration during the first 5 h followed by a slower, but stable, reaction rate in the subsequent hours. A reversible-irreversible kinetic model was applied to explain the degradation rate of CA, its dependence on temperature and concentration. Kinetic parameters for the equilibrium and irreversible reactions were calculated and the proposed kinetic model was validated with experimental data of CA degradation ranging 16.3 mg/L to 127.0 mg/L. Degradation of the chromophore CA-imidazole, which is commonly used for quantifications by High Performance Liquid Chromatography, was also studied at 4 °C and 25 °C, showing a rapid rate of degradation according to irreversible first-order kinetics. A hydrolysis reaction mechanism is proposed as the cause of CA-imidazole loss in aqueous solutions.

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