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CE-ICP-SFMS for the detection of S and Zn in Aeromonas hydrophila Zn-beta-lactamase

Veerle Van Lierde, Karel Strijckmans UGent, M Galleni, Bart Devreese UGent, Jozef Van Beeumen UGent, Frank Vanhaecke UGent and Luc Moens UGent (2003) LC GC EUROPE. 16(9). p.616-620
abstract
Aeromonads are microorganisms that can cause both human and animal infections and is the known source of hospital-acquired infection. Some Aeromonas strains produce metallo-beta-lactamase enzymes, which are at the origin of beta-lactam resistance in members of this genus. The metallo-beta-lactamases are clinically relevant because of their ability to hydrolyse carbapenem antibiotics, and they also represent a relevant investigational model for studying molecular class B beta-lactamases because of their unique enzymological behaviour.(1,2) The Aeromonas hydrophila metallo-beta-lactamase contains Zn as enzymatic cofactor.(3-5) In this work, Zn bound to the metallo-beta-lactamase is separated from free Zn ions by capillary electrophoresis (CE) and the elements Zn and S are detected and quantified simultaneously by use of an inductively coupled plasma-sector field mass spectrometer (ICP-SFMS) operated at medium mass resolution. The goal of this investigation is to develop a method that allows a fast and accurate determination of the Zn/protein ratio. This ratio can be calculated from the Zn/S ratio. The quantification method is limited to proteins where the sulphur stoichiometry is known. The A. hydrophila Zn-beta-lactamase investigated in this work is known to contain 4 methionines and 1 cysteine. For proteins of which the primary structure is unknown, additional structural information is necessary. In this work A. hydrophila Zn-beta-lactamase is being used as proof of concept. Optimum conditions for CE, ICP-SFMS and their hyphenation were investigated. The use of the sodium salt of phytic acid as buffer additive is discussed into more detail.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CAPILLARY-ELECTROPHORESIS, PLASMA-MASS SPECTROMETRY, PHYTIC ACID, METALLOTHIONEIN ISOFORMS, SPECIATION, PROTEINS, RESISTANCE, SEPARATION, RESOLUTION
journal title
LC GC EUROPE
LC GC Eur.
volume
16
issue
9
pages
616 - 620
Web of Science type
Article
Web of Science id
000185914100002
ISSN
1471-6577
language
English
UGent publication?
yes
classification
A1
id
209924
handle
http://hdl.handle.net/1854/LU-209924
date created
2004-04-09 12:29:00
date last changed
2012-11-13 16:29:43
@article{209924,
  abstract     = {Aeromonads are microorganisms that can cause both human and animal infections and is the known source of hospital-acquired infection. Some Aeromonas strains produce metallo-beta-lactamase enzymes, which are at the origin of beta-lactam resistance in members of this genus. The metallo-beta-lactamases are clinically relevant because of their ability to hydrolyse carbapenem antibiotics, and they also represent a relevant investigational model for studying molecular class B beta-lactamases because of their unique enzymological behaviour.(1,2) The Aeromonas hydrophila metallo-beta-lactamase contains Zn as enzymatic cofactor.(3-5) In this work, Zn bound to the metallo-beta-lactamase is separated from free Zn ions by capillary electrophoresis (CE) and the elements Zn and S are detected and quantified simultaneously by use of an inductively coupled plasma-sector field mass spectrometer (ICP-SFMS) operated at medium mass resolution. The goal of this investigation is to develop a method that allows a fast and accurate determination of the Zn/protein ratio. This ratio can be calculated from the Zn/S ratio. The quantification method is limited to proteins where the sulphur stoichiometry is known. The A. hydrophila Zn-beta-lactamase investigated in this work is known to contain 4 methionines and 1 cysteine. For proteins of which the primary structure is unknown, additional structural information is necessary. In this work A. hydrophila Zn-beta-lactamase is being used as proof of concept. Optimum conditions for CE, ICP-SFMS and their hyphenation were investigated. The use of the sodium salt of phytic acid as buffer additive is discussed into more detail.},
  author       = {Van Lierde, Veerle and Strijckmans, Karel and Galleni, M and Devreese, Bart and Van Beeumen, Jozef and Vanhaecke, Frank and Moens, Luc},
  issn         = {1471-6577},
  journal      = {LC GC EUROPE},
  keyword      = {CAPILLARY-ELECTROPHORESIS,PLASMA-MASS SPECTROMETRY,PHYTIC ACID,METALLOTHIONEIN ISOFORMS,SPECIATION,PROTEINS,RESISTANCE,SEPARATION,RESOLUTION},
  language     = {eng},
  number       = {9},
  pages        = {616--620},
  title        = {CE-ICP-SFMS for the detection of S and Zn in Aeromonas hydrophila Zn-beta-lactamase},
  volume       = {16},
  year         = {2003},
}

Chicago
Van Lierde, Veerle, Karel Strijckmans, M Galleni, Bart Devreese, Jozef Van Beeumen, Frank Vanhaecke, and Luc Moens. 2003. “CE-ICP-SFMS for the Detection of S and Zn in Aeromonas Hydrophila Zn-beta-lactamase.” Lc Gc Europe 16 (9): 616–620.
APA
Van Lierde, V., Strijckmans, K., Galleni, M., Devreese, B., Van Beeumen, J., Vanhaecke, F., & Moens, L. (2003). CE-ICP-SFMS for the detection of S and Zn in Aeromonas hydrophila Zn-beta-lactamase. LC GC EUROPE, 16(9), 616–620.
Vancouver
1.
Van Lierde V, Strijckmans K, Galleni M, Devreese B, Van Beeumen J, Vanhaecke F, et al. CE-ICP-SFMS for the detection of S and Zn in Aeromonas hydrophila Zn-beta-lactamase. LC GC EUROPE. 2003;16(9):616–20.
MLA
Van Lierde, Veerle, Karel Strijckmans, M Galleni, et al. “CE-ICP-SFMS for the Detection of S and Zn in Aeromonas Hydrophila Zn-beta-lactamase.” LC GC EUROPE 16.9 (2003): 616–620. Print.