Comparative study of various hydrogen ion buffers to assay Zn(2+)-dependent beta-lactamases

Author:

Benitez M J1,Company M1,Arevalillo A1,Jiménez J S1

Affiliation:

1. Departamento de Química Fisica Aplicada, Universidad Autónoma de Madrid, Spain.

Abstract

The low Zn2+ complex formation constants, the capacity to degrade penicillin G in combination with Zn2+, and UV absorbance make 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, 3-[N-tris(hydroxymethyl)methylamino]-2-hydroxypropanesulfonic acid, 1,3-bis[tris(hydroxymethyl)methylamino]propane, and 1,4-piperazinediethanesulfonic acid convenient buffers to study Zn(2+)-dependent beta-lactamases.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference11 articles.

1. Classification of P-lactamases: groups 1, 2a, 2b, and 2b;Bush K.;Antimicrob. Agents Chemother.,1989

2. Classification of P-lactamases: groups 2c, 2d, 2e, 3, and 4;Bush K.;Antimicrob. Agents Chemother.,1989

3. Methodology for the study of P-lactamases;Bush K.;Antimicrob. Agents Chemother.,1986

4. Separation, purification and properties of 1-lactamase I and P-lactamase II from Bacillus cereus 569/H/9;Davies R. B.;Biochem. J.,1974

5. Metal cofactor requirements of P-lactamase II;Davies R. B.;Biochem. J.,1974

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