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Calorimetric analysis of cephalosporins using an immobilized TEM-1 β-lactamase on Ni<sup>2+</sup>Chelating Sepharose Fast Flow

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dc.contributor.authorRatana Lawungen_US
dc.contributor.authorBengt Danielssonen_US
dc.contributor.authorVirapong Prachayasittikulen_US
dc.contributor.authorLeif Bülowen_US
dc.contributor.otherLunds Universiteten_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-09-07T09:37:49Z
dc.date.available2018-09-07T09:37:49Z
dc.date.issued2001-09-01en_US
dc.description.abstractTwo β-lactamases, penicillinase type I from Bacillus cereus and TEM-1 β-lactamase from Haemophilus ducreyi, were immobilized on a Chelating Sepharose Fast Flow column loaded with Ni2+in an active form. Flow-injection analysis of β-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 β-lactamase were markedly increased upon immobilization for all substrates, especially carbenicillin, cephaloridine, and cefoperazone. © 2001 Academic Press.en_US
dc.identifier.citationAnalytical Biochemistry. Vol.296, No.1 (2001), 57-62en_US
dc.identifier.doi10.1006/abio.2001.5226en_US
dc.identifier.issn00032697en_US
dc.identifier.other2-s2.0-0035450908en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/26451
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035450908&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleCalorimetric analysis of cephalosporins using an immobilized TEM-1 β-lactamase on Ni<sup>2+</sup>Chelating Sepharose Fast Flowen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035450908&origin=inwarden_US

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