MALDI-TOF mass spectra of curcumin complexes with Al(III) were reported by Jiang [73]. As drugs of abuse usage continues to be a problem in the United States, drug testing methodologies using mass spectrometry will continue to be an integral component of the clinical and forensic laboratory. Since molecules fragment in a unique manner, the resulting ion fragmentation pattern can be used to obtain structural information for a given molecule. The applications of LC–MS for quantitative purpose of curcumin and its related compounds in biological samples are described in Table 3.12. Readers should also refer to complementary chapters in this volume on chromatography (chromatographically separated components of mixtures may be fed directly into the MS source for analysis) and proteomics (high-throughput technique for identification and quantification of large sets of proteins by MS (see Chapters 9.11–9.13). This website uses cookies. Site Development: Digital Strategies (Division of Communications) Aid in quantifying low molecular weight drugs and their metabolites in body fluids and tissues using mass spectrometry as core technology. This has been extremely beneficial to biotechnologists who can now observe proteins, peptides, oligosaccharides, DNA fragments, and other large biomolecules. This article is an overview of state-of-the-art technologies involving MS available nowadays to help solve or investigate systems of interest to scientists working in biotechnology-related areas. The wide range of GC-MS application results from the large number of GC-MS instruments installed and the large number of trained users in laboratories around the globe. Such observations have been made possible mostly owing to the advent of two ionization techniques which can bring large, polar, and thermolabile molecules from the solution or solid phase to the gas phase as intact molecular ions. The methodology accomplishes this by combining necessary sensitivity with necessary selectivity and specificity, which is currently unachievable by other platforms. Mass spectrometry (MS) is a high-throughput analytical detection technique used to get information about the molecular weights and chemical structures of the peptides, proteins, carbohydrates, oligonucleotides, natural products, and drug metabolites (Biemann, 2014). Since quantification and identification of the whole metabolome, using one analytical platform is still utopian. In another study, the fragmentation behavior of curcumin and two other compounds was observed using ion trap LC–MS/MS and confirmed with sustained off-resonance irradiation fragmentation (Fourier Transform Ion Cyclotron Resonance (FTICR) SORI-MS/MS) [43]. GC-MS remains highly useful side by side with other analytical platforms for the characterization of biosample metabolomes rendering it an indispensable tool for the analysis of small molecules. Molecular structure determination with MS is not as straightforward as with NMR. Have you noticed this button? Elsevier, Amsterdam, pp. analytical method to find the molecular mass of a compound and indirectly helped to prove the identity of isotopes MS, like NMR, is high throughput, but it is a much more sensitive technique as compounds can be detected in the sub-picomolar range. 187-194. Mass spectrometry is the most widely used methodology in the field of metabolomics (Dunn and Ellis, 2005; Dunn et al., 2005; Khoo and Al-Rubeai, 2007). Figure 5.7. in Practical instrumental analysis / Ed. Elsevier, Amsterdam, blz. It has been applied successfully to a very wide range of analytical problems in the food and nutrition sciences. [75] optimized two different types of MS, the particle beam EI-mass spectra and thermospray mass spectra. Mass spectrometers have become far more accessible, cheaper to purchase and operate, and easier to use, especially over the last decade. J. Krugers and A.I.M. Mass spectrometry Expertise and services The Technology Center for Mass Spectrometry offers high-level expertise in bioanalytical mass spectrometry combined with in-depth knowledge on biomedical and clinical applications, embedded in a cutting-edge clinical and fundamental research environment. There has been increasing variation in the types of acquisition, ionization (for example, electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI)), mass selection (time-of-flight (TOF) Quadrupole and Orbitrap), and detection used based on our expanding knowledge of the proteome.
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