Plasma Source Mass Spectrometry: Current Trends and Future Developments (Special Publications)

ISBN 10: 0854046631 / ISBN 13: 9780854046638

Verlag: Royal Society of Chemistry, 2006

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Inhaltsangabe:

Atomic spectrometry has exciting new bio-analytical horizons open to it, principally through the developments in the capabilities of ICP-MS coupled with the inventiveness of experimentalists. This is reflected in the use of the technique for ion-, capillary electrophoresis-, liquid- and gas-chromatographic separation in biological applications, as reported in this book. Traditional (environmental, semiconductor, geological and clinical) applications are also well represented. In addition, recent and future developments in sample introduction devices, multicollector sector, reaction cells and collision cells instruments, as well as co-existence, divergence and potential convergence of atomic and biomolecular mass spectrometries are discussed. Reflecting the current state of practical ICP-MS and drawing together the latest developments in the field, Plasma Source Mass Spectrometry: Current Trends and Future Developments is ideal for university researchers and laboratory practitioners. It will be of interest to all those involved in the development and application of this technique.

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Plasma Source Mass Spectrometry

Current Trends and Future Developments

By Grenville Holland, Dmitry Bandura

The Royal Society of Chemistry

Copyright © 2005 The Royal Society of Chemistry
All rights reserved.

ISBN: 978-0-85404-663-8

Contents

Bio-analytical Applications, 
Metalloprotein Crosstalk: Quantifying Zinc Exchange Between Stable Isotopically Labeled Proteins Using Directly Coupled HPLC-ICP-MS A.Z. Mason, T.M. Potter, J. Webster and R.F. Meraz, 3, 
Speciation of Selenium Compounds by Capillary Electrophoresis ICP-MS – Evaluation of ICP-DRC-MS Detection and Different Quantification Methods J. Nurmi, G. Koellensperger, G. Stingeder, D. Metze and N. Jakubowski, 28, 
Application of ICPMS and Chromatography Based ICPMS to Studies of Metal-Protein Binding in Bioanalysis D. Gray, R. Burns, P. Brunswick, J. Le Huray, W. Chan, M. Mast, K. Allamneni and S. Sreedharan, 43, 
Determination of Total Mercury in Urine By Inductively Coupled Plasma Mass Spectrometry (ICP-MS) P. Parsons, C. Palmer, K. Caldwell and R. Jones, 59, 
Labile Arsenic Compounds in Biological Matrices, or Possible Problems Finding the Metal Species Present in Cells A. Raab, H. Hansen and J. Feldmann, 72, 
Speciation Analysis with GC-ICP-MS: Organometal Detection in Tobacco Smoke M. Elobeid, Y. Chai, D. Clarke, R. Hannigan and J. Russ, 80, 
Reaction Cells and High Resolution, 
Determination of 44Ca-Isotope Markers for Parasitoid Studies Using Dynamic Reaction Cell ICPMS B. Hattendorf H. Wanner, H. Gu, S. Dorn and D. Gunther, 91, 
Application of ICP-MS with a Hexapole Collision and Reaction Cell as an Element Selective Phosphorus Detector for Quality Control of Pharmaceuticals M. Edler, E. Busker, I. Feldmann, N. Jakubowski and C. Venzago, 99, 
Advantages of Dynamic Reaction Cell ICP-MS for Geological Analyses K. Neubauer, S. Beres, L. Dionne and D. Green, 111, 
Characterization and Production Ratio of Polyatomic Ion Interferences in Inductively Coupled Plasma Mass Spectrometry Using a High Resolution Mass Spectrometer Y. Takaku, D. Hinds and T. Shimamura, 120, 
Measurement of Actinides at Ultra-Trace Level By Double-Focusing Sector-Field ICP-MS: Instrumental Performances and Analytical Difficulties F. Pointurier, N. Baglan and Ph. Hémet, 130, 
Trends in Instrumentation, 
Biomolecular and Atomic Mass Spectrometry: Good Friends or Uncaring Strangers? A. Makarov, 145, 
Love Triangle: Trapping Fields, Ion Energy and Ion Molecule Reactions V. Baranov, D.R. Bandura and S. Tanner, 155, 
Investigation of Vaporization of Laser Ablation Generated Aerosol and Monodisperse Particles in a Dry Ar ICP Using Time-Resolved Mass Spectrometry J. Olesik and N. Casey, 164, 
Environmental Applications, 
Signal Smoothing Device for Improving Analytical Precision in LA-ICP-MS and Its Applications A. Tunheng and T. Hirata, 177, 
Metrology in Chemistry: ICP-Analysis in Environmental Science T. Prohaska, Y. Aregbe and P. Evans, 190, 
ICP-MS as Analytical Tool on Spent Nuclear Fuel Analogues Studies J. Cáceres, J. Quiñones, E. Iglesias and A. Martinez-Esparza, 207, 
Preliminary Work for the LA-ICP-MS Analysis of Carnelian Archaeological Artefacts S. Fraser, D. Polya, P. Lythgoe and T. Insoll, 213, 
Selenium Speciation in Amphibian Larvae Developing in a Coal Fly Ash Settling Basin B. Jackson, W. Hopkins, J. Unrine, J. Baionno and T. Punshon, 225, 
Speciation of Cancerostatic Platinum Compounds in a Waste Water Pilot Plant Zs. Stefánka, S. Hann, K. Lenz, G. Koellensperger, M. Fuerhacker and G. Stingeder, 235, 
Multi-collectors, 
Accurate Determination of Pt Concentrations at Ultra-low Levels (<<20Pg) in Clinical DNA Samples with High HF/PT Ratios Using the Thermo Finnigan Neptune Plasma Ionisation Multi-collector Mass Spectrometer (PIMMS) G. Nowell, D. Pearson, C. Ottley and M. Tilby, 245, 
Novel Applications of MC-ICPMS for Isotope Dilution P. Evans, C. Wolff Briche, R. Hearn and T. Catterick, 259, 
Solution and Laser Ablation Analysis of Sulphur Isotopes with the Neptune High Resolution Multi-collector ICP-MS (MC-ICP-MS): Application to Diffusive Gradients in Thin Films D. Bellis, G. Nowell, C. Ottley, D. Pearson and W. Davison, 268, 
Accuracy and Precision in Plasma Ionisation Multi-collector Mass Spectrometry: Constraints from Neodymium and Hafnium Isotope Measurements D. Pearson and G. Nowell, 284, 
Semiconductors, 
Application of ICP-MS Technology to Semiconductor Manufacturing J.-M. Collard and Y. Kishi, 317, 
Author Index, 334, 
Subject Index, 337, 

CHAPTER 1

Section 1

Bio-analytical Applications

METALLOPROTEIN CROSSTALK: QUANTIFYING ZINC EXCHANGE BETWEEN STABLE ISOTOPICALLY LABELED PROTEINS USING DIRECTLY COUPLED HPLC-ICP-MS

A.Z. Mason, T.M. Potter, J. Webster and R.F. Meraz

Department of Biological Sciences and Institute for Integrated Research in Materials, Environments and Society, California State University, Long Beach, 90840, USA

1 INTRODUCTION

While the importance of Zn as an essential but potentially toxic nutrient has been known for many years, it is only recently, since the completion of the human genome project, that we have come to appreciate just how many genes exhibit putative Zn binding motifs. Conservative estimates indicate perhaps a thousand or more human genes may be zinc regulated and, while we do not yet understand the functioning of many of these proteins, it is clear that Zn is an important cellular signal that can control many aspects of cellular functioning.

1.1 Metallothionein and Trace Metal Homeostasis

One protein that has been advocated to play a central role in intracellular metal metabolism and homeostasis in mammals and other organisms is metallothionein (MT). Metallothioneins (MT's) represent a super gene family of highly conserved proteins that have been implicated in the redox mediated distribution of Zn in animal cells. Four major isoforms of the protein have been identified in humans that are differentially expressed in various tissues. Two of the better-characterized isoforms, termed MT-1 and MT-2, typify the primary structure of the gene family in having a high cysteine content (30%) and no aromatic residues. It is the uniquely high composition of cysteine that accounts for the redox sensitivity of these proteins and their ability to co-ordinate seven Zn or Cd atoms. High resolution X-ray crystallographic studies have shown the protein to have a dumb-bell shape exhibiting 2 metal binding domains. The N-terminal β=domains of each isoform contain nine cysteines coordinating 3 zinc atoms while the C-terminal α-domains are comprised of 11 cysteines, coordinating 4 zinc atoms. The metals are bound tetrahedrally within these domains via thiolate bonds that either form bridges between adjacent metal atoms or act as terminal ligands for the metal. Although these metal-thiol clusters are thermodynamically stable (KD Zn = 1.2 x 10-13 M at pH 7.0), studies have shown that the metal atoms within the cluster are relatively labile, particularly in the β-domain, permitting both intramolecular and intermolecular transfer of Zn within and between given MT isoforms. This apparent lability, which can be increased by the presence of cellular oxidants, also accounts for the ability of the protein to donate Zn to the apo form of various metalloenzymes having a lower affinity for the metal.

1.2 Considerations for Quantifying Transfer of Zn Between Metal-binding...

Bibliografische Details

Titel: Plasma Source Mass Spectrometry: Current ...
Verlag: Royal Society of Chemistry
Erscheinungsdatum: 2006
Einband: Hardcover
Zustand: Neu