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  • P-ISSN2233-4203
  • E-ISSN2093-8950

Vol.8 No.4

Unyong Kim(Chungnam National University, GLYCAN Co., Ltd.,) ; Myung Jin Oh(Chungnam National University) ; Jua Lee(Chungnam National University) ; Hee Yeon Hwang(Chungnam National University) ; Hyun Joo An(Chungnam National University) pp.69-78 https://doi.org/10.5478/MSL.2017.8.4.69
초록보기
Abstract

Glycosylation, which is one of the most common post-translation modification (PTMs) of proteins, plays a variety of crucial roles in many cellular events and biotherapeutics. Recent advances have led to the development of various analytical methods employing a mass spectrometry for glycomic and glycoproteomic study. However, site-specific glycosylation analysis is still a relatively new area with high potential for technologies and method development. This review will cover current MSbased workflows and technologies for site-specific mapping of glycosylation ranging from glycopeptide preparation to MS analysis. Bioinformatic tools for comprehensive analysis of glycoprotein with high-throughput manner will be also included.

Jong Wha Lee(Korea Research Institute of Standard and Science) pp.79-89 https://doi.org/10.5478/MSL.2017.8.4.79
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Abstract

Ion mobility mass spectrometry (IM-MS) combines the advantages of ion mobility spectrometry (IMS) and MS for effective gas-phase ion analysis. Separation of ions based on their mobilities prior to MS can be performed without a great loss in other analytical figures of merit, and the extra dimension of analysis offered by IM can be beneficial for isomer and complex sample analyses. In this review, basic principles of IMS and IM-MS are described in addition to an introduction to various IMS techniques and commercial IM-MS instruments. The nature of collision cross-section (ΩD), an important parameter determining the transport properties of ions in IMS, is also explained in detail.

Saurabh Dubey(National Dope Testing Laboratory) ; Alka Beotra(Anti-Doping Laboratory) pp.90-97 https://doi.org/10.5478/MSL.2017.8.4.90
초록보기
Abstract

Androgenic anabolic steroids (AASs) are synthetic derivatives of testosterone with a common structure containing cyclopentanoperhydrophenanthrene nucleus. Their use enhances the muscle building capacity and is beneficial during performance. The AASs are one of the most abused group of substances in horse doping. Liquid chromatography tandem mass spectrometry (LC/MSn) has been successfully applied to the detection of anabolic steroids in biological samples. However, the saturated hydroxysteroids viz: nandrolone, 5α-estrane-3β, 17α-diol exhibit lower detection responses in electrospray ionisation (ESI) because of their poor ionisation efficiency. To overcome this limitation pre-column chemical derivatization has been introduced to enhance their detection responses in LC-ESI-MSn analysis. The aim of present study was to develop a sensitive method for identification and confirmation of nandrolone and its metabolite in horse urine incorporating pre-column derivatization using picolinic acid. The method consists of extraction of targeted steroid conjugates by solid phase extraction (SPE). The eluted steroid conjugates were hydrolysed by methanolysis and free steroids were recovered with liquid-liquid extraction. The resulting steroids were derivatized to form picolinoyl esters and identification was done using LC-ESI-MS/MS in positive ionization mode. The picolinated steroid adduct enhanced the detection levels in comparison to underivatized steroids.

Jung Jae Jo(Kyungpook National University) ; Lee Sangkyu(Kyungpook National University) pp.98-104 https://doi.org/10.5478/MSL.2017.8.4.98
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Abstract

Ginseng (Panax ginseng Meyer) is a well-known health functional food used as a traditional herbal drug in Asian countries owing to its diverse pharmacological effects. Herb-drug interactions may cause unexpected side effects of co-administered drugs by the alteration of pharmacokinetics through effects on cytochrome P450 activity. In this study, we investigated the herb-drug interactions between Korean red ginseng extract (KRG) and five CYP-specific probes in mice. The pharmacokinetics of KRG extract induced-drug interactions were studied by cassette dosing of five CYP substrates for CYP1A, 2B, 2C, 2D, and 3A and the LC-MS/MS analysis of the blood concentration of metabolites of each of the five probes. The linearity, precision, and accuracy of the quantification method of the five metabolites were successfully confirmed. The plasma concentrations of five metabolites after co-administration of different doses of the KRG extract (0, 0.5, 1, and 2 g/kg) were quantified by LC-MS/MS and dose-dependent pharmacokinetic parameters were determined. The pharmacokinetic parameters of the five metabolites were not significantly altered by the dose of the KRG extract. In conclusion, the single co-administration of KRG extract up to 2 g/kg in vivo did not cause any significant herb-drug interactions linked to the modulation of CYP activity.

Yujin Lee(Hankuk University of Foreign Studies) ; Eunji Seo(Hankuk University of Foreign Studies) ; Tae-Min Park(Hankuk University of Foreign Studies) ; Kwang-Hak Bae(Apple tree Dental Hospital) ; Sangwon Cha(Hankuk University of Foreign Studies) pp.105-108 https://doi.org/10.5478/MSL.2017.8.4.105
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Abstract

Recently, deciduous teeth have been proposed as a promising biomatrix for estimating internal and external chemical exposures of an individual from prenatal periods to early childhood. Therefore, detection of organic chemicals in teeth has received increasing attention. Organic materials in tooth matrix are mostly collagen type proteins, but lipids and other small organic chemicals are also present in the tooth matrix. In this study, matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) was employed to obtain lipid fingerprints from deciduous teeth. Phospholipids and triacylglcerols (TAGs) from deciduous teeth were successfully detected by MALDI MS with 2,5-dihydroxybenzoic acid (DHB) or gold nanoparticle (AuNP) as a matrix.

Dong Yoon Ji(Kookmin University) ; Chang-Wan Lee(Kookmin University) ; Se Hee Park(Yonsei University) ; Eun Jig Lee(Yonsei University) ; Do Yup Lee(Kookmin University) pp.109-113 https://doi.org/10.5478/MSL.2017.8.4.109
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Abstract

Single analytical procedure including extraction, liquid chromatography, and mass spectrometric analysis was evaluated for the simultaneous measurement of lysophospholipids (LPLs). LPLs, particularly, lysophosphatidic acids (LPA) and sphingosine 1-phosphate (S1P) are lipid messengers ubiquitously found in various biological matrix. The molecular species mediate important physiological roles in association with many diseases (e.g. cancer, inflammation, and neurodegenerative disease), which emphasize the significance of the simple and reliable analytical method for biomarker discovery and molecular mechanistic understanding. Thus, we developed analytical method mainly focusing on, but not limited by those lipid species S1P and LPA using reverse phase liquid chromatography-tandem mass spectrometry (RPLC-ESI-MS-MS). Extraction method was modified based on Folch method with optimally minimal level of ionization additive (ammonium formate 10 mM and formic acid). Reverse-phase liquid-chromatography was applied for chromatographical separation in combination with negative ionization mode electrospray-coupled Orbitrap mass spectrometry. The method validation was performed on human blood plasma in a non-targeted lipid profiling manner with full-scan MS mode and data-dependent MS/MS. The proposed method presented good inter-assay precision for primary targets, S1P and LPA. Subsequent analysis of other types of LPLs identified a broad range of lysophosphatidylcholines (LPCs) and lysophosphatidyl-ethanolamines (LPEs).

Ha Ra Cho(Dankook University) ; Sung Giu Jin(Dankook University) ; Jun Seo Park(Dankook University) ; Han Sol Kim(Dankook University) ; Yong Seok Choi(Dankook University) pp.114-118 https://doi.org/10.5478/MSL.2017.8.4.114
초록보기
Abstract

While saliva can be considered as good biological fluid for monitoring biomarkers due to many advantages including its communication with blood and the non-invasive nature during its sampling, its applications to that purpose is still limited. As a part of efforts to expand the applications of saliva to the protein biomarker research, we carried out global absolute quantitation of proteins in human whole saliva (WS) by bottom-up proteomics techniques mainly based on nLC-Q-IMS-TOF employing MSE. From the analyses of a pooled WS sample collected from 22 healthy Korean volunteers, 93 proteins ranging from 5.89×101 ng/mL (immunoglobulin heavy chain) to 1.59×104 ng/mL (α-amylase 1) were confirmed. For the validation of the present results, human serum albumin in the same sample was quantitated by ELISA and its result was compared with that from the nLC-Q-IMS-TOF study. As a result, there was no significant difference between two results from individual approaches (1.18×104 ± 0.03×104 ng/mL from nLC-Q-IMS-TOF experiments vs. 1.23×104 ± 0.07×104 ng/mL from ELISA experiments, n=3, p=0.309). To our knowledge, this is the first global absolute quantitation of proteins in human whole saliva and information from the present study can be widely used as the first level reference for the discovery

Mass Spectrometry Letters