Comparative High-Speed Profiling of Carboxylic Acid Metabolite Levels by Differential Isotope-Coded MALDI Mass Spectrometry

2009 ◽  
Vol 81 (18) ◽  
pp. 7544-7551 ◽  
Author(s):  
Albert Koulman ◽  
Daniel Petras ◽  
Vinod K. Narayana ◽  
Laura Wang ◽  
Dietrich A. Volmer
Author(s):  
Tatsuyuki Kanamori ◽  
Yuki Okada ◽  
Hiroki Segawa ◽  
Tadashi Yamamuro ◽  
Kenji Kuwayama ◽  
...  

Abstract Purpose Recently, the opioid epidemic has become a serious problem, particularly in North America and Europe. The aim of this study was to clarifyQuery the metabolic fate of a new synthetic opioid furanylfentanyl. Methods The metabolism of furanylfentanyl was investigated by incubating fresh human hepatocytes with 10 µM furanylfentanyl at 37 °C for 48 h in an atmosphere of 5% CO2. After incubation, the culture medium was deproteinized and analyzed by liquid chromatography/mass spectrometry. Results On the chromatogram, four metabolites of furanylfentanyl were presumably detected: 4´-hydroxy-furanylfentanyl, β-hydroxy-furanylfentanyl, 4´-hydroxy-3´-methoxy-furanylfentanyl, and a ring-opened carboxylic acid metabolite. These newly found metabolites of furanylfentanyl were then definitely identified using chemically synthesized authentic standards. Conclusions Four metabolites of furanylfentanyl were newly identified. Although it has been proposed over recent years that a dihydrodiol metabolite, which has the same molecular weight as the ring-opened carboxylic acid metabolite, is formed from furanylfentanyl, this study demonstrated that the ring-opened carboxylic acid metabolite, rather than the dihydrodiol metabolite, is formed from furanylfentanyl.


2018 ◽  
Author(s):  
Shazia Khan ◽  
Diego F Cobice ◽  
Dawn EW Livingstone ◽  
C Logan Mackay ◽  
Scott P Webster ◽  
...  

2019 ◽  
Author(s):  
Zachary VanAernum ◽  
Florian Busch ◽  
Benjamin J. Jones ◽  
Mengxuan Jia ◽  
Zibo Chen ◽  
...  

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes, and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is timeconsuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes, or clarified cell lysates. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization.


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