scholarly journals A straightforward gel-free proteomics pipeline assisted by liquid isoelectric focusing (OFFGEL) and mass spectrometry analysis to study bovine meat proteome

2020 ◽  
pp. 108201322092914
Author(s):  
Enrique Sentandreu ◽  
Claudia Fuente-García ◽  
José L Navarro ◽  
Miguel A Sentandreu
Keyword(s):  
Mass Spectrometry ◽  
Isoelectric Focusing ◽  
Quantitative Data ◽  
Ion Trap ◽  
Three Dimensional ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Protein Fractionation ◽  
Spectrometry Analysis ◽  
Proteomic Approach

Bovine sarcoplasmic sub-proteome was studied through a straightforward gel-free pipeline supported by liquid isoelectric focusing (OFFGEL) protein fractionation coupled to liquid chromatography-mass spectrometry (LC-MS) analysis. Full-MS and data-dependent MS/MS analyses were simultaneously performed by a conventional three-dimensional ion-trap addressing targeted quantitative and untargeted qualitative research, respectively. There were unambiguously identified 47 proteins distributed along 12 OFFGEL fractions assayed. Regarding intermediate- and high-abundant peptides, bulky quantitative data processing performed by MZmine 2 freeware yielded a satisfactory linearity and coefficient of variation with r2 in the 0.95–0.99 range and about 25%, respectively. Up to 41 peptides from 20 identified proteins were relatively quantified throughout OFFGEL fractions. This reliable, flexible and affordable gel-free proteomic approach could be readily implemented by industry to improve quality assessment of protein-based food products.

Mass Spectrometry-Based Proteomic Approach in Juglans regia

2021 ◽  
Vol 885 ◽  
pp. 25-31
Author(s):  
Donatella Aiello
Keyword(s):  
Mass Spectrometry ◽  
Juglans Regia ◽  
Maldi Mass Spectrometry ◽  
Mass Spectrometry Analysis ◽  
Intact Protein ◽  
Protein Fractionation ◽  
Spectrometry Analysis ◽  
Protein Mass ◽  
Proteomic Approach ◽  
Mass Information

We proposed a MALDI mass spectrometry based approach to characterize walnut allergens. The strategy is based on the extraction of hydro-soluble tissue proteins followed by protein fractionation and mass-spectrometry analysis. Linear MALDI was adopted to evaluate the intact protein mass information and the presence of glycoproteins.

scholarly journals Effect of Ocular Hypertension on D-β-Aspartic Acid-Containing Proteins in the Retinas of Rats

2019 ◽  
Vol 2019 ◽  
pp. 1-8 ◽  
Author(s):  
Takashi Kanamoto ◽  
Takashi Tachibana ◽  
Yasushi Kitaoka ◽  
Toshio Hisatomi ◽  
Yasuhiro Ikeda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ocular Hypertension ◽  
Aspartic Acid ◽  
Atp Synthase ◽  
Wistar Rats ◽  
Protein Band ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Sds Page

Purpose. To investigate the effect of ocular hypertension-induced isomerization of aspartic acid in retinal proteins. Methods. Adult Wistar rats with ocular hypertension were used as an experimental model. D-β-aspartic acid-containing proteins were isolated by SDS-PAGE and western blot with an anti-D-β-aspartic acid antibody and identified by liquid chromatography-mass spectrometry analysis. The concentration of ATP was measured by ELISA. Results. D-β-aspartic acid was expressed in a protein band at around 44.5 kDa at much higher quantities in the retinas of rats with ocular hypertension than in those of normotensive rats. The 44.5 kDa protein band was mainly composed of α-enolase, S-arrestin, and ATP synthase subunits α and β, in both the ocular hypertensive and normotensive retinas. Moreover, increasing intraocular pressure was correlated with increasing ATP concentrations in the retinas of rats. Conclusion. Ocular hypertension affected the expression of proteins containing D-β-aspartic acid, including ATP synthase subunits, and up-regulation of ATP in the retinas of rats.

scholarly journals Liquid chromatography–mass spectrometry analysis of dyes formed by in situ oxidative methods then purified by absorption and extraction from hair wefts

2020 ◽  
pp. 174751982097862
Author(s):  
M John Plater ◽  
Andrea Raab
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Complex Mixture ◽  
Ammonium Salts ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Chromatography Mass Spectrometry ◽  
Didecyldimethylammonium Chloride

The dye mixtures formed from three commercial hair colour formers were purified by absorption onto human hair wefts, washed and dried, extracted with dichloromethane:trifluoroacetic acid (75:25) and then analysed by liquid chromatography–mass spectrometry. Only 1–2 dyes were identified from each complex mixture of commercial aromatic amines along with a broad UV absorption mainly consisting of mixtures of quaternary ammonium salts from shampoos and some surfactants. Mecetronium ethyl sulfate and didecyldimethylammonium chloride were the main ammonium salts.

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