Calorimetric analysis of cephalosporins using an immobilized TEM-1 beta-lactamase on Ni2+ chelating sepharose fast flow
(2001) In Analytical Biochemistry 296(1). p.57-62- Abstract
Two beta-lactamases, penicillinase type I from Bacillus cereus and TEM-1 beta-lactamase from Haemophilus ducreyi, were immobilized on a Chelating Sepharose Fast Flow column loaded with Ni2+ in an active form. Flow-injection analysis of beta-lactams was performed by using an enzyme column reactor fitted into the enzyme thermistor. With both enzymes it was possible to monitor both penicillins and cephalosporins. Moreover, Michaelis constants of the TEM-1 beta-lactamase were markedly increased upon immobilization for all substrates, especially carbenicillin, cephaloridine, and cefoperazone.
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- author
- Lawung, R LU ; Danielsson, Bengt LU ; Prachayasittikul, V and Bülow, L LU
- organization
- publishing date
- 2001-09-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Anti-Bacterial Agents, Bacillus cereus, Calorimetry, Carbenicillin, Cefoperazone, Cephaloridine, Cephalosporins, Chelating Agents, Chromatography, Affinity, Chromatography, Agarose, Enzymes, Immobilized, Haemophilus ducreyi, Nickel, Penicillinase, Penicillins, beta-Lactamases, beta-Lactams
- in
- Analytical Biochemistry
- volume
- 296
- issue
- 1
- pages
- 6 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:11520032
- scopus:0035450908
- ISSN
- 0003-2697
- DOI
- 10.1006/abio.2001.5226
- language
- English
- LU publication?
- yes
- id
- 3299b0f0-77fc-437a-80ff-cf171500b0f0
- date added to LUP
- 2016-04-18 15:56:22
- date last changed
- 2024-01-04 02:08:52
@article{3299b0f0-77fc-437a-80ff-cf171500b0f0, abstract = {{<p>Two beta-lactamases, penicillinase type I from Bacillus cereus and TEM-1 beta-lactamase from Haemophilus ducreyi, were immobilized on a Chelating Sepharose Fast Flow column loaded with Ni2+ in an active form. Flow-injection analysis of beta-lactams was performed by using an enzyme column reactor fitted into the enzyme thermistor. With both enzymes it was possible to monitor both penicillins and cephalosporins. Moreover, Michaelis constants of the TEM-1 beta-lactamase were markedly increased upon immobilization for all substrates, especially carbenicillin, cephaloridine, and cefoperazone.</p>}}, author = {{Lawung, R and Danielsson, Bengt and Prachayasittikul, V and Bülow, L}}, issn = {{0003-2697}}, keywords = {{Anti-Bacterial Agents; Bacillus cereus; Calorimetry; Carbenicillin; Cefoperazone; Cephaloridine; Cephalosporins; Chelating Agents; Chromatography, Affinity; Chromatography, Agarose; Enzymes, Immobilized; Haemophilus ducreyi; Nickel; Penicillinase; Penicillins; beta-Lactamases; beta-Lactams}}, language = {{eng}}, month = {{09}}, number = {{1}}, pages = {{57--62}}, publisher = {{Elsevier}}, series = {{Analytical Biochemistry}}, title = {{Calorimetric analysis of cephalosporins using an immobilized TEM-1 beta-lactamase on Ni2+ chelating sepharose fast flow}}, url = {{http://dx.doi.org/10.1006/abio.2001.5226}}, doi = {{10.1006/abio.2001.5226}}, volume = {{296}}, year = {{2001}}, }