• 제목/요약/키워드: MALDI-TOF Mass

검색결과 272건 처리시간 0.035초

Effect of Cationization Agent Concentration on Glycan Detection Using MALDI TOF-MS

  • Kim, Inyoung;Shin, Dongwon;Paek, Jihyun;Kim, Jeongkwon
    • Mass Spectrometry Letters
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    • 제8권1호
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    • pp.14-17
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    • 2017
  • The effect of cationization agent concentration on glycan detection via matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) was investigated using $Na^+$ ions in the form of NaCl as the cationization agent. NaCl solution concentrations ranging from 1 mM to 1 M were investigated. Glycans from ovalbumin were mixed with the cationization agent solution and the 2,5-dihydroxybenzoic acid (2,5-DHB) matrix solution in a volume ratio of 1:1:1. The resulting mixture was loaded onto the MALDI plate. Two MALDI-TOF MS instruments (Voyager DE-STR MALDI-TOF MS and Tinkerbell RT MALDI-TOF MS) were used for detection of glycans. The best detection, in terms of the number of identified glycans, the peak intensity, and the signal-to-noise (S/N) ratio, was obtained with NaCl concentrations of 0.01-0.1 M for both MALDI-TOF MS instruments.

Applications of MALDI-TOF Mass Spectrometry in Clinical Microbiology

  • Shin, Kyeong Seob;Yum, Jonghwa
    • 대한의생명과학회지
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    • 제28권3호
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    • pp.145-156
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    • 2022
  • Over the past few decades, few technologies have had a greater impact on clinical microbiology laboratories than matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF MS). The MALDI-TOF MS is a fast, accurate, and low-cost and efficient method of microbial identification. This technology generates characteristic mass spectral fingerprints that is a unique signature for each microorganism, making it an ideal method for accurate identification at the genus and species levels of both bacterial and fastidious microorganism such as anaerobes, mycobacterium and fungi etc. In addition, MALDI-TOF MS has been successfully used in microbial subtyping and susceptibility tests such as determination of resistance genes. In this study, the authors summarized the application of MALDI-TOF MS in clinical microbiology and clinical research and explored the future of MALDI-TOF MS.

Free Radical Initiated Peptide Sequencing Using MALDI-TOF/TOF Mass Spectrometry

  • Song, Insu;Lee, Jae-ung;Baek, Jaehyeon;Cha, Sangwon;Han, Sang Yun;Oh, Han Bin
    • Mass Spectrometry Letters
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    • 제9권2호
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    • pp.56-60
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    • 2018
  • In this study, matrix-assisted laser desorption/ionization (MALDI) was applied to the TEMPO-assisted FRIPS for the first time. We found that 3-HPA is the optimal matrix for the analysis of p-TEMPO-Bz-Sc-peptides, which gives minimal precursor fragmentations. MALDI-TOF/TOF experiments on p-TEMPO-Bz-Sc-peptides yielded mainly $[a_n+H]^+$, $[z_n+H]^+$, and $[y_n]^+-type$ products, indicating that radical-driven peptide fragmentation occurs in MALDI-TOF/TOF-MS.

Analysis of Entamoeba histolytica Membrane via LC-MALDI-TOF/TOF

  • Ujang, Jorim Anak;Noordin, Rahmah;Othman, Nurulhasanah
    • Mass Spectrometry Letters
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    • 제10권3호
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    • pp.84-87
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    • 2019
  • Liquid chromatography mass spectrometry is widely employed in proteomics studies. One of such instruments is the Liquid Chromatography (LC)-Matrix-assisted laser desorption ionisation (MALDI)-Time of flight (TOF) or LC-MALDI-TOF/TOF. In this study, this instrument was used to identify the membrane proteins of a protozoan parasite namely Entamoeba histolytica. It causes amoebiasis in human. The E. histolytica trophozoites were cultured prior to the membrane protein extraction using the conventional method, $ProteoPrep^{(R)}$ and $ProteoExtract^{(R)}$ kits. Then, the membrane protein extracts were trypticdigested and analysed by LC-MALDI-TOF/TOF. Approximately, 194 proteins were identified and 27.8% (54) were predicted as membrane proteins having 1 to 15 transmembrane regions and signal peptides by combining all three extraction methods. Also, this study has discovered 3 unique proteins as compared to our previous study which merit further investigation.

Reliable Identification of Bacillus cereus Group Species Using Low Mass Biomarkers by MALDI-TOF MS

  • Ha, Miyoung;Jo, Hyeon-Ju;Choi, Eun-Kyeong;Kim, Yangsun;Kim, Junsung;Cho, Hyeon-Jong
    • Journal of Microbiology and Biotechnology
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    • 제29권6호
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    • pp.887-896
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    • 2019
  • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)-based pathogen identification relies on the ribosomal protein spectra provided in the proprietary database. Although these mass spectra can discern various pathogens at species level, the spectra-based method still has limitations in identifying closely-related microbial species. In this study, to overcome the limits of the current MALDI-TOF MS identification method using ribosomal protein spectra, we applied MALDI-TOF MS of low-mass profiling to the identification of two genetically related Bacillus species, the food-borne pathogen Bacillus cereus, and the insect pathogen Bacillus thuringiensis. The mass spectra of small molecules from 17 type strains of two bacilli were compared to the morphological, biochemical, and genetic identification methods of pathogens. The specific mass peaks in the low-mass range (m/z 500-3,000) successfully identified various closely-related strains belonging to these two reference species. The intensity profiles of the MALDI-TOF mass spectra clearly revealed the differences between the two genetically-related species at strain level. We suggest that small molecules with low molecular weight, 714.2 and 906.5 m/z can be potential mass biomarkers used for reliable identification of B. cereus and B. thuringiensis.

Construction of an Improved Tandem Time-of-flight Mass Spectrometer for Photodissociation of Ions Generated by Matrix-assisted Laser Desorption Ionization (MALDI)

  • Moon, Jeong-Hee;Yoon, So-Hee;Kim, Myung-Soo
    • Bulletin of the Korean Chemical Society
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    • 제26권5호
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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.

Analysis of nonionic surfactants and silicone polymers in cosmetic products using Matrix - assisted Laser Desorption/Ionization Time-of- flight Mass Spectrometry

  • Lee, Myoung-Hee;Lee, Gae-Ho;Yoo, Jong-Shin
    • 대한화장품학회:학술대회논문집
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    • 대한화장품학회 2003년도 IFSCC Conference Proceeding Book II
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    • pp.480-507
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    • 2003
  • A rapid and efficient method for analyzing the nonionic surfactants and silicone polymers, which control the shape and characteristics of cosmetic products and give influence on product quality, has been developed using Matrix-Assisted Laser Desorption Ionization Time of Flight Mass Spectrometry (MALDI- TOF IMS). The MALDI-TOF/MS could easily and effectively determine the molecular weight distribution and monomer units of nonionic surfactants. As a result, creating a library of mass spectrum data of surfactants used in cosmetic products using MALDI-TOF/MS and analyzing surfactants extracted from the products may become a useful method for detailed structural characterization of the surfactants. Furthermore, the MALDI-TOF/MS analysis was effective in obtaining the spectrum of silicone polymers from which the molecular weight distribution could be determined. The repetition units and structural data could also be obtained through molecular mass peaks. Additionally, the monomer ratio and terminal groups as properties of silicone copolymers could be determined

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$\alpha_1$(I)및 $\alpha_2$(I)사슬 콜라겐의 질량분석법 개발 연구 (Development of mass spectrometric analysis of $\alpha_1$(I) and $\alpha_2$(I) chain Collagen)

  • 김광연;조선영;이상한;남해선;김성호
    • 한국산학기술학회논문지
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    • 제6권2호
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    • pp.134-143
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    • 2005
  • 포유동물에서 중요한 구조단백질인 콜라겐은 다양한 조직내 단백질 조성과 사슬간 복잡한 가교결합의 존재로 인해 그 구조가 복잡하고 다양하여, 직접적으로 분석할 적당한 방법이 없었다. 본 연구에서는 간단한 전처리만으로 다수의 생체분자 시료에 대해 정확한 분자량 측정이 가능한 매트릭스 보조 레이저 탈착/이온화 비행시간 질량분석법(MALDI-TOF MS)을 이용하여 콜라겐과 조각화된 콜라겐을 분석하고 이의 아미노산 서열을 사중극자-비행시간 직렬 질량분석법(Q-TOF MS/MS)으로 확인하여, 시료 중의 콜라겐의 종류에 대한 정보를 확인하여, MALDI-TOF 질량분석을 이용한 콜라겐 분석에서 콜라겐의 종류를 쉽게 예측할 수 있는 방법을 제시하고자 하였다. 쥐의 꼬리에서 분리한 콜라겐을 SDS-PAGE로 분리한 결과 10개의 band를 얻을 수 있었는데, 같은 시료를 MALDI-TOF MS로 확인하여 각 band의 정확한 분자량을 결정할 수 있었다. SDS-PACE상의 10개의 분리된 band에 대해 각각 tryptic digestion후 MALDI-TOF 질량분석을 수행한 결과 4개의 band에서 type I 콜라겐의 $\alpha_1$-chain내의 fragment인 Gly1056-Arg1073을 확인할 수 있었고, 5개의 band에서 type I 콜라겐의 $\alpha_2$-chain내의 fragment인 Gly985-Arg1002을 확인하였다. 잔재한 콜라겐의 가교결합으로 인해 예상되는 fragment중 둘만이 확인되었지만, 확인된 fragment를 통해 적어도 7개의 band에서는 type I콜라겐이 존재함을 확인할 수 있었다. 확인된 두 콜라겐 flagment의 아미노산 서열을 Q-TOF MS/MS로 분석한 결과 MALDI-TOF MS에서의 예측과 일치함을 확인할 수 있었으며, 이를 통해 확인된 두 fragment에 의한 peak을 지문으로 하여 MALDI-TOF MS측정시에 시료내의 type I 콜라겐의 존재를 쉽게 확인할 수 있음을 볼 수 있었다.

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나노물질을 이용한 질량분석 기술 개발동향 (Mass spectrometry based on nanomaterials)

  • 박종민;노주윤;김문주;변재철
    • 세라미스트
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    • 제21권3호
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    • pp.249-269
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    • 2018
  • In conventional MALDI-TOF mass spectrometry, analyte molecules are known to be ionized by mixing with organic matrix molecules. As the organic matrix molecules are made into small fragments, they generate unreproducible mass peaks such that MALDI-TOF mass spectrometry is nearly impossible in the low mass-to-charge (m/z) range (< 1000). Additionally, the dried sample mixed with matrix were made as inhomogeneous crystal on metal plate. When the laser radiation was made on the sample crystal, the amount of generated sample ion was observed to be quite different according to the radiation point. Therefore, the quantitative analysis was very difficult even for the sample spots at the same concentration for the conventional MALDI-TOF mass spectrometry. In this work, we present laser desorption/ionization (LDI) mass spectrometry based on solid-matrices for the quantitative analysis of small molecules in the low m/z range by using MALDI-TOF mass spectrometry: (1) Carbon based nanostructures; (2) Semiconductor based nanomaterials; (3) Metal based nanostructures.

말디토프 질량분석을 이용한 고분자의 특성분석 (Analysis of Polymer Characteristics Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry)

  • 강민정;성윤서;김문주;김명수;변재철
    • 공업화학
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    • 제28권3호
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    • pp.263-271
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    • 2017
  • 최근에, 질량분석기술의 폴리머 분석에의 응용은 MALDI-TOF MS 개발 이후 급속도로 발전하였다. 이 리뷰 논문은 현재까지 연구된 MALDI-TOF MS의 폴리머 특성분석에의 응용에 관한 최신 논문을 정리하였다. MALDI-TOF MS는 바이오 폴리머와, 합성 폴리머의 평균분자량 분석, 폴리머의 시퀀스 분석을 통한 구조의 해석, 모노머의 조성분석에까지 이용되고 있다. 엔드그룹의 특성과 농도를 분석하는 연구도 많이 진행되었고, 복잡한 폴리머의 분자량의 분석에는 SEC와 MALDI-TOF MS를 연결한 분석법을 추천한다. MALDI에 tandem MS를 결합한 분석기술이나, 이온 모빌리티를 응용한 질량분석기, TOF-SIMS, MALDI-TOF-Imaging 기술도 급격히 발전하고 있으며, 이의 폴리머 특성분석에의 응용은 별도의 분리기술이 필요 없어 앞으로 더 많이 이용될 것으로 생각된다. 분자량, 시퀀스, 그리고 모노머의 조성을 정확하게 계산해주는 소프트웨어와 고분자량(> 100 kDa)의 분석을 가능하게 해주는 기술이 개발된다면, 폴리머를 연구하는 과학자들에게 MALDI-TOF MS의 이용은 문제점을 해결하고, 목적하는 폴리머를 합성하는 데 중요한 수단이 될 것이다.