Wild or farmed Gilthead Seabream (Sparus aurata)? How to distinguish between them by two-dimensional gel electrophoresis

2020 ◽  
Author(s):  
Chiara Guglielmetti ◽  
Sonia Brusadore ◽  
Simona Sciuto ◽  
Giovanna Esposito ◽  
Marcello Manfredi ◽  
...  
Keyword(s):  
Protein Extraction ◽  
Sparus Aurata ◽  
Wild Fish ◽  
Gilthead Seabream ◽  
Liver Protein ◽  
Two Dimensional ◽  
Market Demand ◽  
Protein Markers ◽  
Two Dimensional Gel Electrophoresis ◽  
Farmed Gilthead Seabream

As the world wild fish stocks are limited and the market demand increases, fish farming has become an alternative food source and a way to reduce costs for consumers. The sale of farmed as wild fish is a fraudulent practice, it is therefore important to work to provide new and alternative tools that can help in the fight against fraud in order to protect consumers and to ensure food traceability. The proteomic profile of farmed and wild fish differs from one another. With this study we wanted to identify liver protein markers via two-dimensional electrophoresis (2DE) that would allow us to distinguish wild from farmed gilthead seabream.The liver samples from 32 gilthead seabream, wild and farmed, were stored at -80 °C before protein extraction. The samples were subjected to 2DE to detect qualitative and quantitative differences. Proteomic analysis showed a protein spot (molecular weight of ~34 kDa and isoelectric point of ~6.9) only in the samples from the wild gilthead seabream; liquid chromatography tandem mass spectrometry identified the spot as ubiquitin. Ubiquitin could be a valid marker to differentiate wild from farmed gilthead seabream, thus ensuring continuous monitoring throughout the entire commercial chain and fight commercial fraud.

scholarly journals Two-dimensional gel electrophoretic protein profile analysis during seed development of Ocotea catharinensis: a recalcitrant seed species

2010 ◽  
Vol 22 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Leonardo L.C. Dias ◽  
Tiago S. Balbuena ◽  
Vanildo Silveira ◽  
Claudete Santa-Catarina ◽  
Andrej Schevchenko ◽  
...  
Keyword(s):  
Seed Development ◽  
Protein Identification ◽  
Protein Extraction ◽  
Profile Analysis ◽  
Protein Profile ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Recalcitrant Seed ◽  
And Storage ◽  
Cotyledonary Stage

The aim of the present work was to characterize changes in the protein profile throughout seed development in O. catharinensis, a recalcitrant species, by two-dimensional gel electrophoresis. Protein extraction was undertaken by using a thiourea/urea buffer, followed by a precipitation step with 10% TCA. Comparative analysis during seed development showed that a large number of proteins were exclusively detected in each developmental stage. The cotyledonary stage, which represents the transition phase between embryogenesis and the beginning of metabolism related to maturation, presents the highest number of stage-specific spots. Protein identification, through MS/MS analysis, resulted in the identification of proteins mainly related to oxidative metabolism and storage synthesis. These findings contribute to a better understanding of protein metabolism during seed development in recalcitrant seeds, besides providing information on established markers that could be useful in defining and improving somatic embryogenesis protocols, besides monitoring the development of somatic embryos in this species.

Culinary preparation effects on lipid and sensory quality of farmed gilthead seabream (Sparus aurata) and meagre (Argyrosomus regius): An inter-species comparison

2019 ◽  
Vol 301 ◽  
pp. 125263 ◽  
Author(s):  
Niki Alexi ◽  
Dimitra Kogiannou ◽  
Ioanna Oikonomopoulou ◽  
Nick Kalogeropoulos ◽  
Derek V. Byrne ◽  
...  
Keyword(s):  
Sensory Quality ◽  
Sparus Aurata ◽  
Gilthead Seabream ◽  
Species Comparison ◽  
Argyrosomus Regius ◽  
Farmed Gilthead Seabream

A New Method for Proteome Screening with Two-Dimensional Urea-Sds Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Areeba Ahmad ◽  
Riaz Ahmad
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cost Effective ◽  
Polyacrylamide Gel ◽  
Present System ◽  
Liver Protein ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

AbstractTwo-dimensional gel electrophoresis (2DE) separating proteins on the basis of their pI and molecular mass remain the best available technique for protein separation and characterization to date. But due to several limitations, including streak formation in IEF gels, partial solubility of proteins, expensive running conditions and relatively longer time taken, a simple urea-SDS-2D polyacrylamide gel electrophoresis (US2DE) is described here. The system is reasonably sensitive, cost effective with good reproducibility. The method described in this paper employs a chaotropic agent, urea, in the first dimension and sodium dodecyl sulphate (SDS), like conventional system, in the second dimension with an addition of polyacrylamide to screen the liver proteome of healthy and chemically induced fibrotic rats. The system separates the protein on the basis of chargeto- mass ratio and clearly demonstrates differential expression in the liver protein repertoire of healthy and fibrotic rats. Moreover, the present system, like other 2D electrophoretic procedures revealed at least 22 novel spots in the investigated tissues. The technique may be utilized for comprehensive proteome screening of any biological sample and would provide an overview to narrow down the candidate proteins or biomarkers.

Protein extraction from mature rice leaves for two-dimensional gel electrophoresis and its application in proteome analysis

PROTEOMICS ◽  
2004 ◽  
Vol 4 (7) ◽  
pp. 1903-1908 ◽  
Author(s):  
Nazrul Islam ◽  
M. Lonsdale ◽  
N. M. Upadhyaya ◽  
T. J. Higgins ◽  
H. Hirano ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Protein Extraction ◽  
Proteome Analysis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Rice Leaves

scholarly journals Optimized Protocol for Protein Extraction from the Breast Tissue that is Compatible with Two-Dimensional Gel Electrophoresis

2011 ◽  
Vol 5 ◽  
pp. BCBCR.S6263 ◽  
Author(s):  
Olena Zakharchenko ◽  
Christina Greenwood ◽  
Louise Alldridge ◽  
Serhiy Souchelnytskyi
Keyword(s):  
Gel Electrophoresis ◽  
Breast Tissue ◽  
Protein Extraction ◽  
Small Sample Size ◽  
Small Sample ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Main Challenge ◽  
Optimized Protocol ◽  
Separation Of Proteins

Proteomics is a highly informative approach to analyze cancer-associated transformation in tissues. The main challenge to use a tissue for proteomics studies is the small sample size and difficulties to extract and preserve proteins. The choice of a buffer compatible with proteomics applications is also a challenge. Here we describe a protocol optimized for the most efficient extraction of proteins from the human breast tissue in a buffer compatible with two-dimensional gel electrophoresis (2D-GE). This protocol is based on mechanically assisted disintegration of tissues directly in the 2D-GE buffer. Our method is simple, robust and easy to apply in clinical practice. We demonstrate high quality of separation of proteins prepared according to the reported here protocol.

Evaluation of antimicrobials residues in farmed gilthead seabream (Sparus aurata) after administration through medicated feed

Food Control ◽  
2018 ◽  
Vol 86 ◽  
pp. 110-116 ◽  
Author(s):  
João Rosa ◽  
Sara Leston ◽  
Maria Castro ◽  
Andreia Freitas ◽  
Jorge Barbosa ◽  
...  
Keyword(s):  
Sparus Aurata ◽  
Gilthead Seabream ◽  
Farmed Gilthead Seabream
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