• The Journal of Korean Obstetrics and Gynecology
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• v.26 no.4
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• pp.150-168
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• 2013

Purpose: The purpose of this study is to find out the patterns of teenage girls who is easy to suffer from dysmenorrhea with the Inbody test results by Sasang constitutions. Methods: The data from the 1681 participants were collected using a structured menstrual history questionnaire. Based on the survey responses, we had 97 adolescents with menstrual disorder as the test group and 97 adolescents without menstrual disorder as the control group. The clinical trials subjects were asked to respond to another questionnaire for identifying their constitutional types and undergo Inbody test. Results: The result of a comparison of the test and control groups showed that there' no relevance to the body fat mass and body fat percentage with menstrual irregularities. The lesser yang person with menstrual irregularities was no relevance to the body fat percentage. The greater yin person with menstrual irregularities was especially lacking in body fat mass and body fat percentage. The lesser yin person with menstrual irregularities was poor in body fat mass. Conclusions: As for study, female high school students with menstrual disorders have nothing to do with muscle mass. Body fats shortage could pose problems. According to the study, Taeumin female high school students usually needed to higher body fat than a general standard. It seems to be needed more body fat and weight than modern standards in period of poor sexuality for having a normal menorrhea especially Taeumin. It will take some continuing study that BMI standards should be changed or not on the Sasang constitutions.

• Bulletin of the Korean Chemical Society
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• v.35 no.3
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• pp.709-714
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• 2014

Protein tyrosine nitration is considered as an important indicator of nitrosative stresses and as one of the main factors for pathogenesis of inflammation and neuronal degeneration. In this study, we investigated various nitrosative modifications of bovine carbonic anhydrase II (CAII) through qualitative and semi-quantitative analysis using the combined strategy of Fourier transformation ion cyclotron resonance mass spectrometry (FT-ICR MS) and ion-trap tandem mass spectrometry (IT-MS/MS). FT-ICR MS and its spectra were used for the search of the pattern of nitrosative modifications. Identification of nitrosatively modified tyrosine sites were executed through IT-MS/MS. In addition, we also tried to infer the reason for the site-specific nitrosative modifications in CAII. In view of the above purpose, we have explored- i) the side chain accessibility, ii) the electrostatic environment originated from the acidic/basic amino acid residues neighboring to the nitrosatively modified site and iii) the existence of competing amino acid residues for nitration.

• Mass Spectrometry Letters
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• v.3 no.3
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• pp.82-85
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• 2012

The formation of zinc finger peptide-$Zn^{2+}$ complexes in electrospray ionization mass spectrometry (ESI-MS) was examined using three different metal ion sources: $ZnCl_2$, $Zn(CH_3COO)_2$, and $Zn(OOC(CHOH)_2COO)$. For the four zinc finger peptides (Sp1-1, Sp1-3, CF2II-4, and CF2II-6) that bind only a single $Zn^{2+}$ in the native condition, electrospray of apo-zinc finger in solution containing $ZnCl_2$ or $Zn(CH_3COO)_2$ resulted in the formation of zinc finger-$Zn^{2+}$ complexes with multiple zinc ions. This result suggests the formation of nonspecific zinc finger-$Zn^{2+}$ complexes. Zn(tartrate), $Zn(OOC(CHOH)_2COO)$, mainly produced specific zinc finger-$Zn^{2+}$ complexes with a single zinc ion. This study clearly indicates that tartrate is an excellent counter ion in ESI-MS studies of zinc finger-$Zn^{2+}$ complexes, which prevents the formation of nonspecific zinc finger-$Zn^{2+}$ complexes.

• Mass Spectrometry Letters
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• v.9 no.1
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• pp.30-36
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• 2018

A quantitation method for free amino acids in human serum was developed using a stepwise-dilution method and a bimodal cation exchange (CEX)/hydrophilic interaction liquid chromatography (HILIC)-tandem mass spectrometry system equipped with an electrospray ionization source (ESI/MS/MS). This method, which was validated using quality control samples, was optimized for enhanced selectivity and sensitivity. Dithiothreitol (DTT) was used as a reducing agent to prevent the oxidation of a serum sample ($50{\mu}L$), which was then subjected to stepwise dilution using 3, 30, and 90 volumes of acetonitrile containing 0.1% formic acid. Chromatographic separation was performed on an Imtakt Intrada Amino Acid column ($50mm{\times}3mm$, $3{\mu}m$) in mixed mode packed with CEX and HILIC ligands embedded in the stationary phase. Underivatized free amino acids were eluted and separated within 10 min. As a result of the validation, the precision and accuracy for the inter- and intraday assays were determined as 2.11-11.51% and 92.82-109.40%, respectively. The lowest limit of quantification (LLOQ) was $0.5-4.0{\mu}g/mL$ and the matrix effect was 80.22-115.93%. The proposed method was successfully applied to the quantitative analysis of free amino acids in human serum.

• Mass Spectrometry Letters
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• v.15 no.1
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• pp.1-25
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• 2024

Protein glycosylation, a highly significant and ubiquitous post-translational modification (PTM) in eukaryotic cells, has attracted considerable research interest due to its pivotal role in a wide array of essential biological processes. Conducting a comprehensive analysis of glycoproteins is imperative for understanding glycoprotein bio-functions and identifying glycosylated biomarkers. However, the complexity and heterogeneity of glycan structures, coupled with the low abundance and poor ionization efficiencies of glycopeptides have all contributed to making the analysis and subsequent identification of glycans and glycopeptides much more challenging than any other biopolymers. Nevertheless, the significant advancements in enrichment techniques, chromatographic separation, and mass spectrometric methodologies represent promising avenues for mitigating these challenges. Numerous substrates and multifunctional materials are being designed for glycopeptide enrichment, proving valuable in glycomics and glycoproteomics. Mass spectrometry (MS) is pivotal for probing protein glycosylation, offering sensitivity and structural insight into glycopeptides and glycans. Additionally, enhanced MS-based glycopeptide characterization employs various separation techniques like liquid chromatography, capillary electrophoresis, and ion mobility. In this review, we highlight recent advances in enrichment methods and MS-based separation techniques for analyzing different types of protein glycosylation. This review also discusses various approaches employed for glycan release that facilitate the investigation of the glycosylation sites of the identified glycoproteins. Furthermore, numerous bioinformatics tools aiding in accurately characterizing glycan and glycopeptides are covered.

• Journal of the Korean Vacuum Society
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• v.18 no.3
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• pp.197-202
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• 2009

The long term stability of ion current of QMS has been one of key parameters for monitoring gas process in vacuum. The time dependence of ionic current was monitored while the pressure of nitrogen gas was kept at a fixed pressure by introducing the gas into vacuum chamber. The chamber was evacuated to ${\sim}3{\times}10^{-9}\;Torr$ to reduce background signals before the measurement. Two ion sources were tested; one had brownish or black color due to gas contamination and the other one was new, i.e. cleaner. At a nitrogen pressure of $1{\times}10^{-5}\;Torr$, the ionic currents measured by the contaminated ion source decreased faster with time. The decrease rate was respectively ${\sim}46%$ for cleaner one and ${\sim}84%$ for contaminated one after ${\sim}5.5%$ hours. In order to test the effect of filament material on the ion current decrease, we fabricated a tungsten(W) filament which consisted of two parts; one half was made of W and the other was coated with yttria. The similar decrease of ionic currents were shown for the two types of filaments, indicating that slight change of temperature of filament due to material difference i.e. baking effect could not improve the origin of ionic current decrease. Overall the decreasing rate of ionic current is more closely associated with contaminated ion source of QMS rather than its filament materials.

• Journal of the Korean Chemical Society
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• v.37 no.9
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• pp.800-805
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• 1993

An analytical method has been developed to determine trace elements in biological samples. The biological samples are added to a laboratory-bulit Teflon bomb together with nitric acid-hydrogen peroxide mixture and enriched stable isotopes. The samples are decomposed in a microwave oven. The decomposed sample solutions are analyzed by isotope dilution inductively coupled plasma mass spectrometry. The analytical results of the biological samples agree well with the reference values.

• Bulletin of the Korean Chemical Society
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• v.28 no.5
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• pp.745-750
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• 2007

An isotope dilution-liquid chromatography/tandem mass spectrometric method was developed as a candidate reference method for the accurate determination of folic acid in infant milk formula. Sample was spiked with 13C5-folic acid and then extracted with phosphate buffer (pH 6) solution. The extract was further cleaned up by deproteinization followed by a C18 solid-phase extraction cartridge. The extract was analyzed by using LC/ ESI/MS/MS with selectively monitoring the collisionally induced dissociation channels of m/z 442 → m/z 295 and m/z 447 → m/z 295, which are the neutral glutamyl loss from the [M+H]+ ions of folic acid and 13C5-folic acid, respectively. LC/MS/MS chromatograms showed substantially reduced background from chemical noises compared to LC/MS chromatograms. Repeatability and reproducibility studies showed that the LC/MS/ MS method is a reliable and reproducible method which can provide less than 1.5 relative percentage of method precision.

• Bulletin of the Korean Chemical Society
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• v.34 no.1
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• pp.35-41
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• 2013

Metabolic analysis of CR6 interacting factor 1 (Crif1) deficient mouse embryonic fibroblasts with impaired oxidative phosphorylation has been carried out using LC-MS/MS and GC-MS methods. Metabolic profiles of the Crif1 deficient cells were comprehensively obtained for the first time. Loss of oxidative phosphorylation functions in mitochondria resulted in cancer-like metabolic reprogramming with consumption of majority of glucose carbon from up-regulated glycolysis to produce lactate, suppressed utilization of glucose carbon in the TCA cycle, increased amounts of amino acids. The changes in metabolic profile of the Crif1 deficient cells are most probably a consequence of metabolic reprogramming to meet the needs of energy balance and anabolic precursors in compensation for the loss of major oxidative phosphorylation functions.

• Bulletin of the Korean Chemical Society
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• v.34 no.5
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• pp.1401-1406
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• 2013

This study tested the feasibility of observing H/D exchange of intact protein by top-down electron capture dissociation (ECD) mass spectrometry for the investigation of protein structure. Ubiquitin is selected as a model system. Local structural information was obtained from the deuteration levels of c and $z^{\cdot}$ ions generated from ECD. Our results showed that ${\alpha}$-helix region has the lowest deuteration level and the C-terminal fraction containing a highly mobile tail has the highest deuteration level, which correlates well with previous X-Ray and HDX/NMR analyses. We studied site-specific H/D exchange kinetics by monitoring H/D exchange rate of several structural motives of ubiquitin. Two hydrogen bonded ${\beta}$-strands showed similar HDX rates. However, the outer ${\beta}$-strand always has higher deuteration level than the inner ${\beta}$-strand. The HDX rate of the turn structure (residues 8-11) is lower than that of ${\beta}$-strands (residues 1-7 and residues 12-17) it connects. Although isotopic distribution gets broader after H/D exchange which results in a limited number of backbone cleavage sites detected, our results demonstrate that this method can provide valuable detailed structural information of proteins. This approach should also be suitable for the structural investigation of other unknown proteins, protein conformational changes, as well as protein-protein interactions and dynamics.