• Bulletin of the Korean Chemical Society
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• v.23 no.2
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• pp.315-319
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• 2002

Visible surface-assisted desorption/ionization mass spectrometry (SALDI-MS) has been investigated for several small macromolecules deposited on the graphite plate using laser radiation at 532 nm where most of the macromolecules are transparent. The graphite surface functioned well as a photon absorbing material and an energy transfer mediator for visible light. The results show that visible SALDI is a much softer ionization technique than UV-MALDI and FAB-MS in our results with synthetic macromolecules, PPG, PPGMBE and cavitand molecules. For the SALDI of biomolecules, glycerol as a proton source was essential with the graphite plate. As in visible SALDI, the role division of the photon absorbing material and the cationization agent can provide a generality in mass spectrometric analysis of macromolecules compared with MALDI using the dual functional matrix.

• Bulletin of the Korean Chemical Society
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• v.28 no.3
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• pp.427-431
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• 2007

In order to gain insight into the molecular changes at the protein level in plants exposed to low temperature for a long period of time (vernalization), proteome analyses of vernalization-treated Arabidopsis thaliana have been carried out by two-dimensional gel electrophoresis followed by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry. Fourteen proteins including ATP binding/GTP binding/translation elongation factor and glycine-rich RNA-binding protein 7 (GRP7) showed differential expression in vernalization-treated Arabidopsis thaliana. GRP7 showed the most dramatic increase in expression suggesting its involvement in response to vernalization treatment.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.147.2-147.2
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• 2003

A fast and matrix-assisted laser desorption/ionization-mass spectrometry compatible protein staining method in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis is described. It is based on the counterion dye staining method that employs oppositely charged two dyes, Zincon and Ethyl Violet to form an ion-pair complex. It is safe to use since the methanol used previously in staining solution was replaced with ethanol, which is not toxic. The protocol including fixing, staining and quick washing steps can be completed in 1 to 1.5 h depending upon gel thickness. (omitted)

• Bulletin of the Korean Chemical Society
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• v.20 no.7
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• pp.853-856
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• 1999

• Bulletin of the Korean Chemical Society
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• v.26 no.5
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• pp.763-768
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• 2005

An improved tandem time-of-flight (TOF) mass spectrometer for the photodissociation (PD) study of ions generated by matrix-assisted laser desorption ionization (MALDI), MALDI-TOF-PD-TOF, has been designed and constructed. Recording a full spectrum with better than unit mass resolution even in low mass range has been achieved without reflectron voltage stepping which was needed in the previous version. Other aspects of the improvement, such as those in the data system which now allow 10-100 times faster spectral acquisition than with the previous instrument, are described. Rationale for the ideas which have led to the improvements is presented also.

• Journal of Ginseng Research
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• v.45 no.5
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• pp.539-545
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• 2021

Background: Red ginseng polysaccharides (RGPs) have been acknowledged for their outstanding immunomodulation and anti-tumor activities. However, their studies are still limited by the complexity of their structural features, the absence of purification and enrichment methods, and the rarity of the analytical instruments that apply to the analysis of such macromolecules. Thus, this study is an attempt to establish a new mass spectrometry (MS)-based analysis procedure for RGPs. Methods: Saponin pre-excluded powder of RG (RG-SPEP, 10 mg) was treated with 200 µL of distilled water and centrifuged for 5 h at 1000 rpm and 85 ℃. Ethanol-based precipitation and centrifugation were applied to obtain RGPs from the heated extracts. Further, endo-carbohydrase treatments were performed to produce specific saccharide fragments. Solid-phase extraction (SPE) processes were implemented to purify and enrich the enzyme-treated RGPs, while matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF) MS was employed for the partial structural analysis of the obtained RGPs. Results: Utilizing cellulase, porous graphitized carbon (PGC), hydrophilic interaction chromatography (HILIC), and MALDI-TOF/TOF MS, the neutral and acidic RGPs were qualitatively analyzed. Hex_n and Hex_n-18 (cellulose analogs) were determined to be novel neutral RGPs. Additionally, the [Unknown + Hex_n] species were also determined as new acidic RGPs. Furthermore, HexA_n (H) was determined as another form of the acidic RGPs. Conclusion: Compared to the previous methods of analysis, these unprecedented applications of HILIC-SPE and MALDI-TOF/TOF MS to analyze RGPs proved to be fairly effective for fractionating and detecting neutral and acidic components. This new procedure exhibits great potential as a specific tool for searching and determining various polysaccharides in many herbal medicines.

• Mass Spectrometry Letters
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• v.4 no.1
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• pp.21-23
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• 2013

The effects of trifluoroacetic acid (TFA) were evaluated on the generation of multiply charged ions of cytochrome c in a 2-nitrophloroglucinol (2-NPG) matrix in high-vacuum, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The presence of 1% TFA in the 2-NPG matrix solution was more effective in generating multiply charged protein ions than matrix solutions containing 0.1% or 0% TFA. Regarding the matrix itself, with 1% TFA, 2-NPG was significantly more effective in generating multiply charged ions than 2,5-dihydroxybenzoic acid (2,5-DHB). The maximum charge state of cytochrome c was +8 when using a 2-NPG matrix containing 1% TFA.

• Bulletin of the Korean Chemical Society
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• v.17 no.11
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• pp.1036-1039
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• 1996

Synthetic lipoidal peptides based on viral protein sequences have been prepared. These peptides contain an N-palmitoyl group at the N-terminal residue, which is a modified cysteine, containing a S-[2,3-bis(acyloxy)-(2-R,S)-propyl] moiety. When this residue (Pam3Cys) is at the N-terminus of a synthetic peptide, it acts as potent immunoadjuvant to enhance both IgM and IgG antibody responses to the attached peptide. Conventional analytical procedures (e.g., Edman degradation and amino acid analysis) are either not applicable due to the N-terminal modification, or do not provide confirmation of the intact structure. Chromatographic analysis is also hindered by the tendency of these lipoidal Pam3Cys peptides to form large aggregates, and in some cases to be permanently adsorbed on reversed phase columns. We have applied several mass spectrometric techniques, including fast atom bombardment (FAB), electrospray ionization (ESI) and matrix assisted laser desorption ionization (MALDI) to characterize the intact structures of a number of different Pam3Cys synthetic peptides. The MALDI-MS has been found to be the most sensitive for the analysis of the structure of Pam3Cys peptides.

• Mass Spectrometry Letters
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• v.2 no.2
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• pp.53-56
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• 2011

[ $C_8$ ]functionalized magnetic nanoparticles were synthesized by coating magnetic $Fe_3O_4$ nanoparticles with silicaamine groups using 3-aminopropyltriethoxysilane and by subsequently modifying the amine groups with chloro(dimethyl)octylsilane to produce octyl groups on the surface of the MNPs. The $C_8$-functionalized MNPs were used to enrich peptides from tryptic protein digests of myoglobin and ${\alpha}$-casein. The enriched peptides were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). MALDI-MS was also used to investigate desalting of the $C_8$-functionalized MNPs. Sample solutions were prepared in 1.0 M NaCl, and the successful removal of salt was observed. Enrichment with $C_8$-functionalized MNPs was very effective for separating and concentrating tryptic peptides.

• Bulletin of the Korean Chemical Society
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• v.34 no.9
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• pp.2635-2639
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• 2013

The rapid and accurate identification of biological agents is a critical step in the case of bio-terror and biological warfare attacks. Recently, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry has been widely used for the identification of microorganisms. In this study, we describe a method for the rapid and accurate discrimination of Bacillus anthracis spores using MALDI-TOF MS. Our direct in-situ analysis of MALDI-TOF MS does not involve subsequent high-resolution mass analyses and sample preparation steps. This method allowed the detection of species-specific biomarkers from each Bacillus spores. Especially, B. anthracis spores had specific biomarker peaks at 2503, 3089, 3376, 6684, 6698, 6753, and 6840 m/z. Cluster and PCA analyses of the mass spectra of Bacillus spores revealed distinctively separated clusters and within-groups similarity. Therefore, we believe that this method is effective in the real-time identification of biological warfare agents such as B. anthracis as well as other microorganisms in the field.