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Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue
INTRODUCTION. Rapigest is an acid-labile detergent used in proteomics for the improvement of protein digestion. MATERIALS AND METHOD. To test the efficacy of Rapigest for proteomics analysis of different sample types we used protein extracts from S9 cell line and mouse heart tissue and performed pro...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Iuliu Hatieganu University of Medicine and Pharmacy
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620675/ https://www.ncbi.nlm.nih.gov/pubmed/26528033 http://dx.doi.org/10.15386/cjmed-367 |
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author | POP, CRISTINA MOGOSAN, CRISTINA LOGHIN, FELICIA |
author_facet | POP, CRISTINA MOGOSAN, CRISTINA LOGHIN, FELICIA |
author_sort | POP, CRISTINA |
collection | PubMed |
description | INTRODUCTION. Rapigest is an acid-labile detergent used in proteomics for the improvement of protein digestion. MATERIALS AND METHOD. To test the efficacy of Rapigest for proteomics analysis of different sample types we used protein extracts from S9 cell line and mouse heart tissue and performed protein isolation, digestion and mass spectrometry analysis. RESULTS: For the S9 cell line, there was no significant difference concerning the number of identifications (peptides, proteins) between Rapigest and No Rapigest samples, though slightly more peptides and proteins were identified in the Rapigest samples. For the mouse heart tissue samples, Rapigest use resulted in the identification of a higher number of proteins. Rapigest did not modify the protein profile with respect to the biological compartments covered by the identified proteins in S9 cell line samples, but produced a small increase in the representation of cytoplasm proteins and a small decrease in the representation of membrane proteins in the mouse heart tissue samples. DISCUSSIONS. Results are comparable to other studies that evaluated the efficacy of Rapigest for the analysis of tissue samples, recommending Rapigest for the improvement of protein digestion and implicitly identification, without the modification of the protein profile in the samples. CONCLUSION. Rapigest may be successfully used for the improvement of protein identification from heart tissue samples using mass spectrometry. |
format | Online Article Text |
id | pubmed-4620675 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Iuliu Hatieganu University of Medicine and Pharmacy |
record_format | MEDLINE/PubMed |
spelling | pubmed-46206752015-11-02 Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue POP, CRISTINA MOGOSAN, CRISTINA LOGHIN, FELICIA Clujul Med Original Research INTRODUCTION. Rapigest is an acid-labile detergent used in proteomics for the improvement of protein digestion. MATERIALS AND METHOD. To test the efficacy of Rapigest for proteomics analysis of different sample types we used protein extracts from S9 cell line and mouse heart tissue and performed protein isolation, digestion and mass spectrometry analysis. RESULTS: For the S9 cell line, there was no significant difference concerning the number of identifications (peptides, proteins) between Rapigest and No Rapigest samples, though slightly more peptides and proteins were identified in the Rapigest samples. For the mouse heart tissue samples, Rapigest use resulted in the identification of a higher number of proteins. Rapigest did not modify the protein profile with respect to the biological compartments covered by the identified proteins in S9 cell line samples, but produced a small increase in the representation of cytoplasm proteins and a small decrease in the representation of membrane proteins in the mouse heart tissue samples. DISCUSSIONS. Results are comparable to other studies that evaluated the efficacy of Rapigest for the analysis of tissue samples, recommending Rapigest for the improvement of protein digestion and implicitly identification, without the modification of the protein profile in the samples. CONCLUSION. Rapigest may be successfully used for the improvement of protein identification from heart tissue samples using mass spectrometry. Iuliu Hatieganu University of Medicine and Pharmacy 2014 2014-11-12 /pmc/articles/PMC4620675/ /pubmed/26528033 http://dx.doi.org/10.15386/cjmed-367 Text en http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License |
spellingShingle | Original Research POP, CRISTINA MOGOSAN, CRISTINA LOGHIN, FELICIA Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title | Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title_full | Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title_fullStr | Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title_full_unstemmed | Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title_short | Evaluation of Rapigest Efficacy for the Digestion of Proteins from Cell Cultures and Heart Tissue |
title_sort | evaluation of rapigest efficacy for the digestion of proteins from cell cultures and heart tissue |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620675/ https://www.ncbi.nlm.nih.gov/pubmed/26528033 http://dx.doi.org/10.15386/cjmed-367 |
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