Characterization of low molecular weight components of [(ViMe2SiO1/2)x(PhSiO3/2)y(SiO4/2)z], [(ViMe2SiO1/2)x(SiO4/2)y], and [(SiO4/2)x(HO1/2)y(tBuO1/2)z] silsesquioxanes by electrospray ionization fourier transform mass spectrometry (ESI-FTMS)

2005 ◽  
Vol 16 (4) ◽  
pp. 524-534 ◽  
Author(s):  
Huiping Chen ◽  
Duane R. Bujalski ◽  
Kai Su
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Fourier Transform ◽  
Electrospray Ionization ◽  
Fourier Transform Mass Spectrometry ◽  
Low Molecular Weight ◽  
Electrospray Ionization Fourier Transform

scholarly journals Advantages of Molecular Weight Identification during Native MS Screening

Planta Medica ◽  
2018 ◽  
Vol 84 (16) ◽  
pp. 1201-1212
Author(s):  
Ahad Khan ◽  
Anne Bresnick ◽  
Sean Cahill ◽  
Mark Girvin ◽  
Steve Almo ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Fourier Transform ◽  
T Cell ◽  
Electrospray Ionization ◽  
Fourier Transform Mass Spectrometry ◽  
Protein Complexes ◽  
Native Mass Spectrometry ◽  
Biochanin A ◽  
Electrospray Ionization Fourier Transform

AbstractNative mass spectrometry detection of ligand-protein complexes allowed rapid detection of natural product binders of apo and calcium-bound S100A4 (a member of the metal binding protein S100 family), T cell/transmembrane, immunoglobulin (Ig), and mucin protein 3, and T cell immunoreceptor with Ig and ITIM (immunoreceptor tyrosine-based inhibitory motif) domains precursor protein from extracts and fractions. Based on molecular weight common hits were detected binding to all four proteins. Seven common hits were identified as apigenin 6-C-β-D-glucoside 8-C-α-L-arabinoside, sweroside, 4′,5-dihydroxy-7-methoxyflavanone-6-C-rutinoside, loganin acid, 6-C-glucosylnaringenin, biochanin A 7-O-rutinoside and quercetin 3-O-rutinoside. Mass guided isolation and NMR identification of hits confirmed the mass accuracy of the ligand in the ligand-protein MS complexes. Thus, molecular weight ID from ligand-protein complexes by electrospray ionization Fourier transform mass spectrometry allowed rapid dereplication. Native mass spectrometry using electrospray ionization Fourier transform mass spectrometry is a tool for dereplication and metabolomics analysis.

Identification of peptides from sinus gland extracts in the red swampcrayfish Procambarus clarkii by mass spectrometry

2016 ◽  
Author(s):  
XIN ZHOU ◽  
YAN SHUI ◽  
Zeng-Hong XU
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
Electrospray Ionization ◽  
Fourier Transform Mass Spectrometry ◽  
Procambarus Clarkii ◽  
Decapod Crustacean ◽  
Peptide Hormone ◽  
Sinus Gland ◽  
Electrospray Ionization Fourier Transform ◽  
Neuroendocrine Organ

Crustacean sinus gland (SG) is a well-defined neuroendocrine organ that controls the secretion of various neuropeptides which regulate many physiological activities. The red swamp crayfish Procambarus clarkii is a decapod crustacean with both high economic and scientific importance in China. To facilitate physiological investigations of SG peptide/hormone function in this species, we have been employed tissue extract fractionation by HPLC to obtain a complete description of neuropeptidome and used Electrospray ionization-Fourier transform mass spectrometry (ESI-FTMS) to detect the peptidome present in its organ. In total, 48 peptide sequences belonging to several known neuropeptide families including crustacean cardioactive peptide, CHH precursor-related peptides (CPRPs), orcokinins and pigment dispersing hormones were identified. Among these 48 sequences, 26 are novel peptides and 22 are previously identified. Overall, the results give a stimulus for future physiological studies of SG neuropeptides in P. clarkii and other crustaceans.

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