Modified general affinity adsorbent for large-scale purification of penicillinases

Kiss, László; Tar, Andrea; Gál, Susanne; Toth-Martinez, Bela L.; Hernádi, F.

doi:10.1016/s0021-9673(01)84569-6

Cited by 7 publications

(3 citation statements)

References 9 publications

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“…The presence of oxacillin-hydrolyzing ß-lactamase in all of these strains was proved by measuring the hydrolysis of oxacillin in suspension of whole cells. To clarify whether the oxacillin-hydrolyzing activity was extracellular or membrane-bound, we purified extracellular enzymes and isolated membranes according to our methods described previously [17,18]. The purified extracellular enzymes were highly active on nitrocefin but failed to hydrolyze oxacillin to any detectable extent, whereas membranes isolated from each of the four strains showed definite oxacillin-hydrolyzing activity (table 3).…”

Section: Discussionmentioning

confidence: 99%

“…Preparation of the N-acetyl-D-penicillamineSepharose 4B affinity adsorbent and purification of the enzymes were done according to the method of Kiss [17], except that the bacteria were cultured in 1% CY broth with 0.5 Ìg/ml methicillin as inducer.…”

Section: Purification Of ß-Lactamases By Affinity Chromatographymentioning

confidence: 99%

“…In the present experiments, our aim was to demonstrate and partially characterize ß-lactamases active on PRPs in borderlinephenotype S. aureus with methods different from those applied by the above authors [9]. For this purpose, we wanted to make use of our previously described methods for the purification of ß-lactamase enzymes [17] and isolation of bacterial membranes [18], applying globomycin as a test substance with a well-defined effect on the processing of prelipoproteins in bacteria [15,16]. …”

Section: Introductionmentioning

confidence: 99%

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Investigation of Oxacillin-Hydrolyzing Beta-Lactamase in Borderline Methicillin-Resistant Clinical Isolates of <i>Staphylococcus aureus</i>

et al. 2001

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Background: Mechanisms of borderline resistance of Staphylococcus aureus to penicillinase-resistant penicillins (PRPs) may include hyperproduction of classical penicillinase and/or production of β-lactamase hydrolyzing also PRPs. Methods: β-Lactamase activity of whole cells and purified enzymes was estimated spectrophotometrically and in isolated cytoplasmic membranes by bioassay with Bacillus subtilis as test strain. Results: Out of 53 clinical isolates of S. aureus, 18 showed oxacillin MIC values from 0.5 to 2 µg/ml, which were reduced by sulbactam and/or clavulanic acid in the case of four isolates producing large quantities of inducible, type A β-lactamase. Cytoplasmic membranes isolated from these strains showed oxacillin-hydrolyzing activity. One of these strains was grown also in the presence of globomycin, an antibiotic known to interfere with the anchorage of membrane lipoproteins; this treatment eliminated the oxacillin-hydrolyzing activity. Conclusions: The resistance in these strains was due to a membrane-bound lipoprotein with oxacillin-hydrolyzing activity.

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Section: Discussionmentioning

confidence: 99%

Section: Purification Of ß-Lactamases By Affinity Chromatographymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Investigation of Oxacillin-Hydrolyzing Beta-Lactamase in Borderline Methicillin-Resistant Clinical Isolates of <i>Staphylococcus aureus</i>

et al. 2001

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Affinity Chromatography

Batista‐Viera¹,

Janson²,

Carlsson³

2011

Methods of Biochemical Analysis

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Two types of resin-conjugated Tamiflu analogs were synthesized by modifying our original synthetic route of oseltamivir phosphate (Tamiflu). The prepared resins bound to influenza virus neuraminidase, the main target of Tamiflu. The resins will be useful for isolating and identifying presumed endogenous vertebrate proteins that interact with Tamiflu, which might relate to the rarely observed abnormal behavior exhibited by some influenza patients treated with Tamiflu.

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