Liquid chromatography-mass spectrometry.  Coupling of a liquid chromatograph to a mass spectrometer

Lovins, R. E.; Ellis, Shane R.; Tolbert, G. D.; McKinney, C. R.

doi:10.1021/ac60330a045

Cited by 49 publications

(12 citation statements)

References 8 publications

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“…The obvious disadvantages include impairment of analytical resolution by working with chromatographic fractions and time consumption in the manual procedure. To solve the last problem, Lovins et al 26 developed an on-line semiautomatic device based on a motor-driven solid probe. The column eluent was collected in a probe reservoir and then transported to a probe tip made of a gold gauze matrix or an active sorbent (charcoal).…”

Section: Interfaces That Eliminate the Solventmentioning

confidence: 99%

The coupling of gas and liquid chromatography with mass spectrometry

Abian

1999

J. Mass Spectrom.

112

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Section: Interfaces That Eliminate the Solventmentioning

confidence: 99%

The coupling of gas and liquid chromatography with mass spectrometry

Abian

1999

J. Mass Spectrom.

112

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“…There has been very little discussion relating to the use of liquid chromatography (LC) as a powerful separation technique in this review up until now. Despite first being described almost half a century prior to GC (Tswett, ), it took another 40 years before it became a useful separation tool following development by Martin and Synge (one part of the group who went on to develop GC 10 years later; Martin & Synge, ), and a further 30 years before LC was successfully coupled with a mass spectrometer (Lovins et al, ). By this time, GC‐MS had long been established and was already a widespread technique within laboratories.…”

Section: Analytical Developments Driving Methodological Progressmentioning

confidence: 99%

Historical and contemporary stable isotope tracer approaches to studying mammalian protein metabolism

Wilkinson

2016

Mass Spectrometry Reviews

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Over a century ago, Frederick Soddy provided the first evidence for the existence of isotopes; elements that occupy the same position in the periodic table are essentially chemically identical but differ in mass due to a different number of neutrons within the atomic nucleus. Allied to the discovery of isotopes was the development of some of the first forms of mass spectrometers, driven forward by the Nobel laureates JJ Thomson and FW Aston, enabling the accurate separation, identification, and quantification of the relative abundance of these isotopes. As a result, within a few years, the number of known isotopes both stable and radioactive had greatly increased and there are now over 300 stable or radioisotopes presently known. Unknown at the time, however, was the potential utility of these isotopes within biological disciplines, it was soon discovered that these stable isotopes, particularly those of carbon (13C), nitrogen (15N), oxygen (18O), and hydrogen (2H) could be chemically introduced into organic compounds, such as fatty acids, amino acids, and sugars, and used to “trace” the metabolic fate of these compounds within biological systems. From this important breakthrough, the age of the isotope tracer was born. Over the following 80 yrs, stable isotopes would become a vital tool in not only the biological sciences, but also areas as diverse as forensics, geology, and art. This progress has been almost exclusively driven through the development of new and innovative mass spectrometry equipment from IRMS to GC‐MS to LC‐MS, which has allowed for the accurate quantitation of isotopic abundance within samples of complex matrices. This historical review details the development of stable isotope tracers as metabolic tools, with particular reference to their use in monitoring protein metabolism, highlighting the unique array of tools that are now available for the investigation of protein metabolism in vivo at a whole body down to a single protein level. Importantly, it will detail how this development has been closely aligned to the technological development within the area of mass spectrometry. Without the dedicated development provided by these mass spectrometrists over the past century, the use of stable isotope tracers within the field of protein metabolism would not be as widely applied as it is today, this relationship will no doubt continue to flourish in the future and stable isotope tracers will maintain their importance as a tool within the biological sciences for many years to come. © 2016 The Authors. Mass Spectrometry Reviews Published by Wiley Periodicals, Inc. Mass Spec Rev

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“…It was consequent to the introduction of the electrospray ionization (ESI) source that the implementation of capillary electrophoresis (CE), as a separation technique prior to mass spectrometry (MS) analysis, was investigated alongside liquid chromatography (LC) . Indeed, similarly to matrix‐assisted laser desorption/ionization (MALDI), ESI unlocked the formation of ions from polar molecules especially biological molecules like peptides and proteins.…”

Section: Introductionmentioning

confidence: 99%

Revealing the potential of capillary electrophoresis/mass spectrometry: the tipping point

Gahoual

Leize‐Wagner

Houzé

et al. 2018

Rapid Comm Mass Spectrometry

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The hyphenation of capillary electrophoresis and mass spectrometry (CE/MS) remains a minor technique compared with liquid chromatography/mass spectrometry (LC/MS), which represents nowadays the standard instrumentation, regardless of its introduction thirty years ago. However, from a theoretical point of view, CE coupling should be quite favorable especially with electrospray ionization mass spectrometry (ESI-MS). At the time, the sensitivity provided by CE/MS was often limited, due to hyphenation requirements, which at some point appeared to disqualify CE/MS from benefiting from the performance gain driving the evolution of MS instruments. However, this context has been significantly modified in a matter of a few years. The development of innovative CE/MS interfacing systems has enabled an important improvement regarding sensitivity and reinforced robustness in order to provide an instrumentation accessible to the largest scientific community. Because of the unique selectivity delivered by the electrophoretic separation, CE/MS has proved to be particularly relevant for the analysis of biological molecules. The conjunction of these aspects is motivating the interest in CE/MS analysis and shows that CE/MS is mature enough to enrich the toolbox of analytical techniques for the analysis of complex biological samples. Here we discuss the characteristics of the major types of high-sensitivity CE/ESI-MS instrumentation and emphasize the late evolution and future positioning of CE/MS analysis for the characterization of biological molecules like peptides and proteins, through some pertinent applications.

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Liquid chromatography-mass spectrometry. Coupling of a liquid chromatograph to a mass spectrometer

Cited by 49 publications

References 8 publications

The coupling of gas and liquid chromatography with mass spectrometry

The coupling of gas and liquid chromatography with mass spectrometry

Historical and contemporary stable isotope tracer approaches to studying mammalian protein metabolism

Revealing the potential of capillary electrophoresis/mass spectrometry: the tipping point

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