What can electrospray mass spectrometry of paratungstates in an equilibrating mixture tell us?

RSC Advances ◽  
2015 ◽  
Vol 5 (101) ◽  
pp. 83377-83382 ◽  
Author(s):  
Linyuan Fan ◽  
Jie Cao ◽  
Changwen Hu
Keyword(s):  
Mass Spectrometry ◽  
Aqueous Solution ◽  
Raman Spectroscopy ◽  
Electrospray Mass Spectrometry ◽  
Esi Ms ◽  
Main Species

[W7O24]6−, the main species in an aqueous solution of Na2WO4at pH ≤ 7 proved by NMR and Raman spectroscopy, fails to be detected in ESI-MS due to its ESI-induced dissociation into Lindqvist [W6O19]2−.

Formation and hydrolysis of polynuclear Th(IV) complexes – a nano-electrospray mass-spectrometry study

2008 ◽  
Vol 96 (7) ◽  
Author(s):  
C. Walther ◽  
M. Fuss ◽  
S. Büchner
Keyword(s):  
Mass Spectrometry ◽  
Aqueous Solution ◽  
Electrospray Mass Spectrometry ◽  
Mass Spectrometry Study ◽  
Hydrolysis Of

Polynuclear hydroxide complexes play an important role for the hydrolysis of tetravalent thorium ions in aqueous solution, in particular for Th(IV) concentrations exceeding some [Th(IV)]=10

scholarly journals Application of Capillary Electrophoresis Mass Spectrometry and Liquid Chromatography Multiple-Step Tandem Electrospray Mass Spectrometry To Profile Glycoform Expression during Haemophilus influenzae Pathogenesis in the Chinchilla Model of Experimental Otitis Media

2008 ◽  
Vol 76 (7) ◽  
pp. 3255-3267 ◽  
Author(s):  
Susanna L. Lundström ◽  
Jianjun Li ◽  
Martin Månsson ◽  
Marisol Figueira ◽  
Magali Leroy ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Liquid Chromatography ◽  
Sialic Acid ◽  
Haemophilus Influenzae ◽  
Otitis Media ◽  
Electrospray Mass Spectrometry ◽  
Esi Ms ◽  
Nthi Strain ◽  
Multiple Step

ABSTRACT Otitis media caused by nontypeable Haemophilus influenzae (NTHi) is a common and recurrent bacterial infection of childhood. The structural variability and diversity of H. influenzae lipopolysaccharide (LPS) glycoforms are known to play a significant role in the commensal and disease-causing behavior of this pathogen. In this study, we determined LPS glycoform populations from NTHi strain 1003 during the course of experimental otitis media in the chinchilla model of infection by mass spectrometric techniques. Building on an established structural model of the major LPS glycoforms expressed by this NTHi strain in vitro (M. Månsson, W. Hood, J. Li, J. C. Richards, E. R. Moxon, and E. K. Schweda, Eur. J. Biochem. 269:808-818, 2002), minor isomeric glycoform populations were determined by liquid chromatography multiple-step tandem electrospray mass spectrometry (LC-ESI-MS n ). Using capillary electrophoresis ESI-MS (CE-ESI-MS), we determined glycoform profiles for bacteria from direct middle ear fluid (MEF) samples. The LPS glycan profiles were essentially the same when the MEF samples of 7 of 10 animals were passaged on solid medium (chocolate agar). LC-ESI-MS n provided a sensitive method for determining the isomeric distribution of LPS glycoforms in MEF and passaged specimens. To investigate changes in LPS glycoform distribution during the course of infection, MEF samples were analyzed at 2, 5, and 9 days postinfection by CE-ESI-MS following minimal passage on chocolate agar. As previously observed, sialic acid-containing glycoforms were detected during the early stages of infection, but a trend toward more-truncated and less-complex LPS glycoforms that lacked sialic acid was found as disease progressed.

Use of Electrospray Mass Spectrometry (ESI-MS) for the Study of Europium(III) Complexation with Bis(dialkyltriazinyl)pyridines and Its Implications in the Design of New Extracting Agents

2002 ◽  
Vol 41 (26) ◽  
pp. 7031-7041 ◽  
Author(s):  
Sonia Colette ◽  
Badia Amekraz ◽  
Charles Madic ◽  
Laurence Berthon ◽  
Gérard Cote ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Esi Ms ◽  
Extracting Agents

Cucurbit[7]uril host-guest complexes with cationic bis(4,5-dihydro-1H-imidazol-2-yl) guests in aqueous solution

2006 ◽  
Vol 84 (6) ◽  
pp. 905-914 ◽  
Author(s):  
D Saroja N Hettiarachchi ◽  
Donal H Macartney
Keyword(s):  
Mass Spectrometry ◽  
Aqueous Solution ◽  
Nmr Spectroscopy ◽  
Stability Constants ◽  
Electrospray Mass Spectrometry ◽  
Hydrophobic Core ◽  
Guest Complex ◽  
H Nmr ◽  
Host Guest Complex ◽  
Proton Resonances

The host–guest interactions between cucurbit[7]uril and a series of novel cationic bis(4,5-dihydro-1H-imidazol-2-yl)arene and 1-(4,5-dihydro-1H-imidazol-2-yl)- and 1,3-bis(4,5-dihydro-1H-imidazol-2-yl)-adamantane guests have been investigated in aqueous solution using UV–vis and NMR spectroscopy, and electrospray mass spectrometry. With the exception of the 1,3-bis(4,5-dihydro-1H-imidazol-2-yl)adamantane (which binds externally to the CB[7]), these guests form very stable inclusion complexes with slow exchange on the 1H NMR timescale. The direction and magnitude of the complexation-induced shifts (CIS) in the proton resonances of the guests are indicative of the residence of the hydrophobic core of the guest within the CB[7] cavity and the charged 4,5-dihydro-1H-imidazol-2-yl units outside the cavity adjacent to the carbonyl-lined portals of the host. The CIS values and the inclusion stability constants have been correlated with the nature of the guest core and with the distance between the charges on the terminal 4,5-dihydro-1H-imidazol-2-yl rings.Key words: cucurbit[7]uril, host–guest complex, dihydroimidazolyl, inclusion stability constants.

scholarly journals Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins

Metallomics ◽  
2018 ◽  
Vol 10 (4) ◽  
pp. 587-594 ◽  
Author(s):  
Marija Nišavić ◽  
Goran V. Janjić ◽  
Amela Hozić ◽  
Marijana Petković ◽  
Miloš K. Milčić ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Serum Albumin ◽  
Binding Sites ◽  
Electrospray Mass Spectrometry ◽  
Integrated Approach ◽  
Docking Studies ◽  
Esi Ms ◽  
Negative Mode

Negative mode nanoLC/nano ESI MS was used for determing Ru(ii) binding sites on protein.

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