Mechanism investigation of HS radical and CS losses from positively charged biradicals of diphenyl sulfides by APCI mass spectrometry

2016 ◽  
Vol 30 ◽  
pp. 2-7
Author(s):  
Xiaoji Cao ◽  
Chenlu Wang ◽  
Weimin Mo

2014 ◽  
Vol 20 (2) ◽  
pp. 169-175 ◽  
Author(s):  
David Bongiorno ◽  
Serena Indelicato ◽  
Gianluca Giorgi ◽  
Simona Scarpella ◽  
Vincenzo Turco Liveri ◽  
...  


2012 ◽  
Vol 132 (1) ◽  
pp. 525-531 ◽  
Author(s):  
Yvonne Chukwumah ◽  
Lloyd Walker ◽  
Bernhard Vogler ◽  
Martha Verghese


2020 ◽  
Author(s):  
Shuli Tang ◽  
Licheng Fan ◽  
Heyong Cheng ◽  
Xin Yan

In this study, we developed an AC-induced interfacial electro-epoxidation reaction for localization of double-bonds in nega-tively and positively charged forms of lipids simultaneously. An AC voltage plays multiple roles in this method, including initiation of the electrochemical epoxidation of double-bonds in both charge states of lipids, and protonation and deprotona-tion of lipid for detection in both ion modes. The advantages of simultaneous detection of negatively changed and positively charged unsaturated lipids, voltage-controlled electrochemical derivatization, and the low sample consumption allow its wide applications in a broad range of lipid-related research.



Eisei kagaku ◽  
1992 ◽  
Vol 38 (2) ◽  
pp. 162-167 ◽  
Author(s):  
MICHIAKI TATSUNO ◽  
MAYUMI NISHIKAWA ◽  
MUNEHIRO KATAGI ◽  
HITOSHI TSUCHIHASHI ◽  
KAZUO IGARASHI ◽  
...  


2007 ◽  
Vol 30 (1) ◽  
pp. 89-94 ◽  
Author(s):  
Shama P. Mirza ◽  
Brian D. Halligan ◽  
Andrew S. Greene ◽  
Michael Olivier

Membrane-bound and membrane-associated proteins are difficult to analyze by mass spectrometry, since the association with lipids impedes the isolation and solubilization of the proteins in buffers suitable for mass spectrometry and the efficient generation of positively charged peptide ions by electrospray ionization. Current methods mostly utilize detergents for the isolation of proteins from membranes. In this study, we present an improved detergent-free method for the isolation and mass spectrometric identification of membrane-bound and membrane-associated proteins. We delipidate proteins from the membrane bilayer by chloroform extraction to overcome dissolution and ionization problems during analysis. Comparison of our results to results obtained by direct tryptic digestion of insoluble membrane pellets identifies an increased number of membrane proteins, and a higher quality of the resulting mass spectral data.



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