Peer Reviewed: Characterizing Synthetic Polymers by MALDI MS

Wu, Kuang Jen; Odom, Robert W.

doi:10.1021/ac981910q

Cited by 105 publications

(74 citation statements)

References 26 publications

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“…(J Am Soc Mass Spectrom 2002, 13, 1015-1027) © 2002 American Society for Mass Spectrometry S ince its inception and commercial availability, the versatility of MALDI-TOFMS has been demonstrated convincingly by its extensive use for qualitative analysis. For example, MALDI-TOFMS has been employed for the characterization of synthetic polymers [1,2], peptide and protein analysis [3][4][5], DNA and oligonucleotide sequencing [6 -8], and the characterization of recombinant proteins [9,10]. Recently, applications of MALDI-TOFMS have been extended to include the direct analysis of biological tissues and single cell organisms with the aim of characterizing endogenous peptide and protein constituents [11][12][13][14][15][16][17][18].…”

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confidence: 99%

Practical quantitative biomedical applications of MALDI-TOF mass spectrometry

Bucknall

Fung

Duncan

2002

J. Am. Soc. Mass Spectrom.

159

136

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Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS) is used to obtain fast and accurate determinations of molecular mass, but quantitative determinations are generally made by other techniques. In this study we illustrate the practical utility of automated MALDI-TOFMS as a tool for quantifying a diverse array of biomolecules covering an extensive molecular weight range, and present in biological extracts and fluids. Growth hormone was measured in rat pituitary tissue; insulin in human pancreatic tissue; homovanillic acid in human urine; and LVV-hemorphin-7, epinephrine and norepinephrine in human adrenal and pheochromocytoma tissues. Internal standards including compounds of similar molecular weight, structural analogs or isotopomers were incorporated into each analysis. We report on the current practical limitations of quantitative MALDI-TOFMS and highlight some of the potential benefits of this technique as a quantitative tool. (J Am Soc Mass Spectrom 2002, 13, 1015-1027) © 2002 American Society for Mass Spectrometry S ince its inception and commercial availability, the versatility of MALDI-TOFMS has been demonstrated convincingly by its extensive use for qualitative analysis. For example, MALDI-TOFMS has been employed for the characterization of synthetic polymers [1,2], peptide and protein analysis [3][4][5], DNA and oligonucleotide sequencing [6 -8], and the characterization of recombinant proteins [9,10]. Recently, applications of MALDI-TOFMS have been extended to include the direct analysis of biological tissues and single cell organisms with the aim of characterizing endogenous peptide and protein constituents [11][12][13][14][15][16][17][18].The properties that make MALDI-TOFMS a popular qualitative tool-its ability to analyze molecules across an extensive mass range, high sensitivity, minimal sample preparation and rapid analysis times-also make it a potentially useful quantitative tool. MALDI-TOFMS also enables non-volatile and thermally labile molecules to be analyzed with relative ease. It is therefore prudent to explore the potential of MALDI-TOFMS for quantitative analysis in clinical settings, for toxicological screenings, as well as for environmental analysis. In addition, the application of MALDI-TOFMS to the quantification of peptides and proteins is particularly relevant. The ability to quantify intact proteins in biological tissue and fluids presents a particular challenge in the expanding area of proteomics and investigators urgently require methods to accurately measure the absolute quantity of proteins.While there have been reports of quantitative MALDI-TOFMS applications, there are many problems inherent to the MALDI ionization process that have restricted its widespread use [19 -39]. These limitations primarily stem from factors such as the sample/matrix heterogeneity that is believed to contribute to the large variability in observed signal intensities for analytes, the limited dynamic range due to detector saturation, and difficulties associated ...

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confidence: 99%

Practical quantitative biomedical applications of MALDI-TOF mass spectrometry

Bucknall

Fung

Duncan

2002

J. Am. Soc. Mass Spectrom.

159

136

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“…Hence, SEEC provides an alternative for the characterization of polymers with reduced solvent and sample consumption. In addition, coupling of CEC with MS may provide an absolute method of MW determination that overcomes the sample bias issues associated with direct MALDI MS of polydisperse polymeric samples [72,73].…”

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Size‐exclusion capillary electrochromatographic separation of polysaccharides using polymeric stationary phases

2003

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We report the successful size-based separations of large, neutral polysaccharides using capillary electrochromatography (CEC). As the polysaccharides possessed little chromophore for photometric detection, two separate approaches were taken. In the first approach, indirect detection was combined with size-exclusion chromatography using a sulfonated polystyrene/divinylbenzene stationary phase. The separations were performed using a 300 Å pore size stationary phase under aqueous conditions. Nonsize based interactions were minimal using this material, resulting in an effective calibration range of molecular masses 180 to 112 000 g?mol 21 for pullulans. In the second approach, the polysaccharides were derivatized with phenylisocyanate and were subsequently separated on columns made using a combination of high capacity ionexchanger and a neutral polystyrene/divinylbenzene material of various pore sizes. The sulfonated ion-exchange phase provided the electroosmotic flow, while the mixed pore size material provided the extended calibration range. The linear range for this primarily nonaqueous system using tetrahydrofuran was determined to be from molecular masses 738 to 404 000 g?mol 21 of the original, untagged pullulan. This approach overcame the limited solubility issue associated with analysis of some polysaccharides. Analysis of pullulan and amylose samples by CEC correlated well with results obtained by conventional high-performance liquid chromatography (HPLC). The sizeexclusion electrochromatographic separations provide an alternative mode for determining the relative molecular weights of polysaccharides with reduced sample and solvent consumption, as well as analysis times.

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“…In this study, the MALDI-TOF analysis confirmed the mass and thus helped to establish the COP-BIP structure. Because of the tendency of MALDI-TOF mass spectrometry to favor the ionization of lower molecular weight species, the spectra of these oligomers should not be considered to represent the true molecular weight distribution [24].…”

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confidence: 99%