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

Issued Date

2001-09-01

Resource Type

Article

ISSN

00032697

DOI

10.1006/abio.2001.5226

Other identifier(s)

2-s2.0-0035450908

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Analytical Biochemistry. Vol.296, No.1 (2001), 57-62

Suggested Citation

Ratana Lawung, Bengt Danielsson, Virapong Prachayasittikul, Leif Bülow Calorimetric analysis of cephalosporins using an immobilized TEM-1 β-lactamase on Ni<sup>2+</sup>Chelating Sepharose Fast Flow. Analytical Biochemistry. Vol.296, No.1 (2001), 57-62. doi:10.1006/abio.2001.5226 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/26451

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Title

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

Author(s)

Ratana Lawung
 Bengt Danielsson
 Virapong Prachayasittikul
 Leif Bülow

Other Contributor(s)

Lunds Universitet
 Mahidol University

Abstract

Two 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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

Availability

URI

https://repository.li.mahidol.ac.th/handle/20.500.14594/26451

Collections

Scopus 2001-2005