Seasonal variations in the profile of main phospholipids in Mytilus galloprovincialis mussels: A study by hydrophilic interaction liquid chromatography-electrospray ionization Fourier transform mass spectrometry

2017 ◽  
Vol 53 (1) ◽  
pp. 1-20 ◽  
Author(s):  
Laura Facchini ◽  
Ilario Losito ◽  
Tommaso R.I. Cataldi ◽  
Francesco Palmisano
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
Liquid Chromatography ◽  
Electrospray Ionization ◽  
Seasonal Variations ◽  
Mytilus Galloprovincialis ◽  
Fourier Transform Mass Spectrometry ◽  
Hydrophilic Interaction Liquid Chromatography ◽  
Hydrophilic Interaction ◽  
Electrospray Ionization Fourier Transform

scholarly journals Tracing the Thermal History of Seafood Products through Lysophospholipid Analysis by Hydrophilic Interaction Liquid Chromatography–Electrospray Ionization Fourier Transform Mass Spectrometry

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2212 ◽  
Author(s):  
Ilario Losito ◽  
Laura Facchini ◽  
Rosa Catucci ◽  
Cosima Calvano ◽  
Tommaso Cataldi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
Liquid Chromatography ◽  
Electrospray Ionization ◽  
Fourier Transform Mass Spectrometry ◽  
Hydrophilic Interaction Liquid Chromatography ◽  
Thermal Treatments ◽  
Hydrophilic Interaction ◽  
Seafood Products ◽  
History Of

Low temperature treatments commonly applied to seafood products have been shown to influence their phospholipid (PL) profile through enzymatic hydrolysis. In the present study, the generation of lysophospholipids (LPL) resulting from this process was systematically investigated for selected, commercially relevant seafood products, namely oysters, clams, octopuses, and shrimps. These products were subjected to thermal treatments like refrigeration or freezing after being purchased as fresh, defrozen, or frozen products depending on the case. The coupling between hydrophilic interaction liquid chromatography (HILIC) and electrospray ionization with high resolution/accuracy Fourier transform mass spectrometry (ESI-FTMS) was exploited to evaluate the PL profile of the cited products, especially the incidence of LPL related to the two main PL classes of seafood products—phosphatidylcholines (PC) and phosphatidylethanolamines (PE)—in the lipid extracts. The lyso forms of PE (LPE) were found to be generally more sensitive than those of PC (LPC) to thermal treatments, usually exhibiting a significant increase upon prolonged refrigeration at 4 °C in all types of investigated products except European flat oysters. Moreover, the distinction between fresh and frozen or defrozen products could be achieved in the case of octopuses and shrimps, respectively.

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.

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