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Figure 3. Workflow of MALDI-TOF MS based species identification. The bacterial single colony is added to the target plate and the resulting characteristic mass peak profile is compared to
a reference database. [Source: Dierig et al 2015]
Figure 4. Scheme of the steps involved in a proteomics experiment. [Source: Susnea et al 2013]
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Figure 5. scheme for identification of bioactive ingredients in TCMs by MALDI-TOF MS [Source: Lu and Cai 2013].
step and to optimize the reaction conditions prior to electrospray ionization (ESI)
analysis or as a supportive tool to complement ESI data [16].
Concluding Remarks
MALDI-TOF MS has been developed
considerably in recent years and now constitutes a quantum leap in the identification of pathogenic microbes and is also a
powerful tool for the detection and localization of drugs, proteins, and lipids in tissue. The technology provides a very rapid,
cost-effective, easy-to-use and reliable detection method. However, MALDI-TOF
MS applications can go far beyond their
current use. Identification directly from
complex clinical specimens such as urine
or cerebrospinal fluid can make a timely
difference in the management of patients
with severe infections whereas identification of the DNA profiles and expression
of biomarkers in bodily fluids such as venous blood, saliva, and semen has contributed greatly to forensic investigations. In
addition, the future potential of this technology has not been completely explored,
and novel applications are currently being
developing, such as rapid pathogen typing
for outbreak situations, early detection of
Figure 6. Scheme outlining the different steps involved for profiling and imaging mass spectrometry of mammalian tissue samples [Source:
Chaurand et al 2004].
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4.
Tadros, M. and A. Petrich, Evaluation
of MALDI-TOF mass spectrometry and
Sepsityper Kit for the direct identification
of organisms from sterile body fluids in a
Canadian pediatric hospital. Can J Infect
Dis Med Microbiol. 24(4): p. 191-4.
5. Jamal, W., R. Saleem, and V.O. Rotimi,
Rapid identification of pathogens directly
from blood culture bottles by Bruker matrix-assisted laser desorption laser ionization-time of flight mass spectrometry
versus routine methods. Diagn Microbiol
Infect Dis. 76(4): p. 404-8.
6. Susnea, I., et al., Application of MALDI-TOF-mass spectrometry to proteome
analysis using stain-free gel electrophoresis. Top Curr Chem. 331: p. 37-54.
7. An, J.H., et al., Body fluid identification in
forensics. BMB Rep. 45(10): p. 545-53.
8. Pusch, W., et al., MALDI-TOF mass spectrometry-based SNP genotyping. Pharmacogenomics, 2002. 3(4): p. 537-48.
9. Donfack, J. and A. Wiley, Mass spectrometry-based cDNA profiling as a potential
tool for human body fluid identification.
Forensic Sci Int Genet. 16C: p. 112-120.
10. Kemptner, J., et al., GEMMA and MALDI-TOF MS of reactive PEGs for pharmaceutical applications. J Pharm Biomed
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