CENTA as a chromogenic substrate for studying β-lactamases

被引：90

作者：

Bebrone, C

Moali, C

Mahy, F

Rival, S

Docquier, JD

Rossolini, GM

Fastrez, J

Pratt, RF

Frère, JM

Galleni, M ^{[1
]}

机构：

[1] Univ Liege, Inst Chim B6, Ctr Prot Engn, B-4000 Liege, Belgium

[2] Univ Catholique Louvain, Lab Biochim Phys & Biopolymeres, B-1348 Louvain, Belgium

[3] Univ Saarlandes, Fachrichtung Biochem 8 8, D-66123 Saarbrucken, Germany

[4] Univ Siena, Dipartimento Biol Mol, Sez Microbiol, I-53100 Siena, Italy

[5] Wesleyan Univ, Dept Chem, Middletown, CT 06459 USA

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2001年 / 45卷 / 06期

关键词：

D O I：

10.1128/AAC.45.6.1868-1871.2001

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

CENTA, a chromogenic cephalosporin, is readily hydrolyzed by B-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta -lactamase-producing strains on agar plates, it should be quite useful for kinetic studies and the detection of the enzymes in crude extracts and chromatographic fractions.

引用

页码：1868 / 1871

页数：4

共 23 条

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