NDLI: Capillary electrophoresis hyphenated to inductively coupled plasma-sector field-mass spectrometry for the stoichiometric determination of Zn bound to <i>Aeromonas hydrophila</i> Zn beta-lactamase

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Capillary electrophoresis hyphenated to inductively coupled plasma-sector field-mass spectrometry for the stoichiometric determination of Zn bound to Aeromonas hydrophila Zn beta-lactamase

Content Provider	Royal Society of Chemistry (RSC)
Author	Vanhaecke, Frank Beeumen, Jozef Van Lierde, Veerle Van Strijckmans, Karel Devreese, Bart Galleni, Moreno Chéry, Cyrille C. Moens, Luc
Copyright Year	2004
Abstract	A method was developed for the determination of the stoichiometric Zn/protein ratio for the Aeromonas hydrophila metallo beta-lactamase AE036. Capillary electrophoresis (CE) was used to separate free Zn ions from the Zn bound to the metalloprotein, the only Zn-species which is biochemically relevant. An inductively coupled plasma-sector field-mass spectrometer (ICP-SF-MS), operated at a mass resolution of 3000, was used as an element-specific detector. If the primary structure of the protein and thus the number of sulfur-containing amino acids is known, as is the case for Aeromonas hydrophila Zn beta-lactamase, monitoring of both Zn and S with ICP-SF-MS permits the Zn/protein ratio to be determined. The method was optimised in order to obtain short migration times (less than 10 min) for the metallo beta-lactamase and for standards with bare fused silica capillaries. After optimisation, a 75 mmol L−1 bis-Tris background electrolyte buffered at a pH of 6.75 was used for the separation, a voltage of 30 kV was applied over a capillary with a total length of approximately 70 cm and the sample was introduced hydrodynamically at 1000 mbar s. Quantitative results (stoichiometric Zn/protein ratio of 1 and 2, before and after saturation of the enzyme with Zn, respectively) were obtained using external calibration with albumin as a S standard and ZnCl2 as a Zn standard. The method was also demonstrated to be precise with < 5% RSD on the Zn/protein ratio for n = 3. An absolute limit of detection of 8 ng of A. hydrophila Zn beta-lactamase (calculated on the basis of sulfur) was obtained under these conditions.
Starting Page	888
Ending Page	893
Page Count	6
File Format	HTM / HTML PDF
ISSN	02679477
Volume Number	19
Issue Number	7
Journal	Journal of Analytical Atomic Spectrometry
DOI	10.1039/b400962b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Aeromonas Stoichiometry Protein Aeromonas hydrophila Metallo Beta-lactamase Capillary electrophoresis Metalloprotein Spectrometer Fused quartz Capillary action Electrolyte PH Bar (unit) Enzyme Albumin Sulfur
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Analytical Chemistry

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Capillary electrophoresis hyphenated to inductively coupled plasma-sector field-mass spectrometry for the stoichiometric determination of Zn bound to Aeromonas hydrophila Zn beta-lactamase