scholarly journals Transforming presumptive forensic testing: in situ identification and age estimation of human bodily fluids

2019 ◽  
Vol 10 (4) ◽  
pp. 1064-1069 ◽  
Author(s):  
Stephanie Rankin-Turner ◽  
Matthew A. Turner ◽  
Paul F. Kelly ◽  
Roberto S. P. King ◽  
James C. Reynolds
Keyword(s):  
Mass Spectrometry ◽  
Age Estimation ◽  
Rapid Identification ◽  
New Method ◽  
Bodily Fluids ◽  
Sampling Probe ◽  
Forensic Testing

A new method utilising an in situ sampling probe coupled with mass spectrometry for rapid identification and age estimation of biofluids.

In vivo endoscopic mass spectrometry using a moving string sampling probe

The Analyst ◽  
2017 ◽  
Vol 142 (15) ◽  
pp. 2735-2740 ◽  
Author(s):  
Lee Chuin Chen ◽  
Tsubasa Naito ◽  
Satoru Tsutsui ◽  
Yuki Yamada ◽  
Satoshi Ninomiya ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Transportation System ◽  
Sampling Probe

A novel moving string sampling probe and sample transportation system for performing in situ and in vivo endoscopic MS.

Rapid identification of the “smart drug” modafinil in suspicious tablets by DART-HRMS combined with micropunching

2020 ◽  
Vol 12 (11) ◽  
pp. 1430-1440 ◽  
Author(s):  
Liying Zhou ◽  
Xin Wang ◽  
Wanhui Liu ◽  
Ping Xiang ◽  
Hang Chen
Keyword(s):  
Mass Spectrometry ◽  
Thermal Instability ◽  
Rapid Identification ◽  
New Method ◽  
Mass Spectrometry Analysis ◽  
Real Case ◽  
Illegal Trade ◽  
Spectrometry Analysis ◽  
Smart Drug

Modafinil, with the name “smart drug”, sometimes is “invisible” in conventional forensic mass spectrometry analysis, by its thermal instability. Because of this, the illegal trade in it is rampant. Now we have new method to detect it in real case.

Optics-Free Visualization of Proteins in Single Cells by Time of Flight-Secondary Ion Mass Spectrometry Coupled with Genetically Encoded Chemical Tags

2020 ◽  
Author(s):  
Feifei Jia ◽  
Jie Wang ◽  
Yanyan Zhang ◽  
Qun Luo ◽  
Luyu Qi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Single Cells ◽  
Time Of Flight ◽  
E Coli ◽  
Tof Sims ◽  
Ion Mass Spectrometry ◽  
Chemical Tags ◽  
Secondary Ion

<p></p><p><i>In situ</i> visualization of proteins of interest at single cell level is attractive in cell biology, molecular biology and biomedicine, which usually involves photon, electron or X-ray based imaging methods. Herein, we report an optics-free strategy that images a specific protein in single cells by time of flight-secondary ion mass spectrometry (ToF-SIMS) following genetic incorporation of fluorine-containing unnatural amino acids as a chemical tag into the protein via genetic code expansion technique. The method was developed and validated by imaging GFP in E. coli and human HeLa cancer cells, and then utilized to visualize the distribution of chemotaxis protein CheA in E. coli cells and the interaction between high mobility group box 1 protein and cisplatin damaged DNA in HeLa cells. The present work highlights the power of ToF-SIMS imaging combined with genetically encoded chemical tags for <i>in situ </i>visualization of proteins of interest as well as the interactions between proteins and drugs or drug damaged DNA in single cells.</p><p></p>

Chicken Pituitary Glycoproteins: New Isolation Method

1999 ◽  
Vol 64 (9) ◽  
pp. 1510-1516
Author(s):  
Helena Ryšlavá ◽  
Jana Krešlová ◽  
Jana Barthová ◽  
Tomislav Barth
Keyword(s):  
Mass Spectrometry ◽  
Luteinizing Hormone ◽  
New Method ◽  
Hormonal Activity ◽  
Isolation Method ◽  
Molecular Weights ◽  
Testosterone Production ◽  
Maldi Tof ◽  
Tryptic Cleavage

A new method for isolation of glycoproteins from chicken pituitaries was applied. The procedure consist of chromatography on ConA-Sepharose and by HPLC on S Hyper D and Vydac C4 columns. The hormonal activity of the glycoproteins was tested by determining their stimulatory effect on cAMP or testosterone production. Molecular weights of the products of tryptic cleavage of the hormone were determined using mass spectrometry (MALDI TOF). A comparison of the values obtained with theory shows that the protein is the β-unit of chicken luteinizing hormone.

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