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In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos
BACKGROUND: Hen's egg white has been the subject of intensive chemical, biochemical and food technological research for many decades, because of its importance in human nutrition, its importance as a source of easily accessible model proteins, and its potential use in biotechnological processes...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041730/ https://www.ncbi.nlm.nih.gov/pubmed/21299891 http://dx.doi.org/10.1186/1477-5956-9-7 |
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author | Mann, Karlheinz Mann, Matthias |
author_facet | Mann, Karlheinz Mann, Matthias |
author_sort | Mann, Karlheinz |
collection | PubMed |
description | BACKGROUND: Hen's egg white has been the subject of intensive chemical, biochemical and food technological research for many decades, because of its importance in human nutrition, its importance as a source of easily accessible model proteins, and its potential use in biotechnological processes. Recently the arsenal of tools used to study the protein components of egg white has been complemented by mass spectrometry-based proteomic technologies. Application of these fast and sensitive methods has already enabled the identification of a large number of new egg white proteins. Recent technological advances may be expected to further expand the egg white protein inventory. RESULTS: Using a dual pressure linear ion trap Orbitrap instrument, the LTQ Orbitrap Velos, in conjunction with data analysis in the MaxQuant software package, we identified 158 proteins in chicken egg white with two or more sequence unique peptides. This group of proteins identified with very high confidence included 79 proteins identified in egg white for the first time. In addition, 44 proteins were identified tentatively. CONCLUSIONS: Our results, apart from identifying many new egg white components, indicate that current mass spectrometry technology is sufficiently advanced to permit direct identification of minor components of proteomes dominated by a few major proteins without resorting to indirect techniques, such as chromatographic depletion or peptide library binding, which change the composition of the proteome. |
format | Text |
id | pubmed-3041730 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30417302011-02-19 In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos Mann, Karlheinz Mann, Matthias Proteome Sci Research BACKGROUND: Hen's egg white has been the subject of intensive chemical, biochemical and food technological research for many decades, because of its importance in human nutrition, its importance as a source of easily accessible model proteins, and its potential use in biotechnological processes. Recently the arsenal of tools used to study the protein components of egg white has been complemented by mass spectrometry-based proteomic technologies. Application of these fast and sensitive methods has already enabled the identification of a large number of new egg white proteins. Recent technological advances may be expected to further expand the egg white protein inventory. RESULTS: Using a dual pressure linear ion trap Orbitrap instrument, the LTQ Orbitrap Velos, in conjunction with data analysis in the MaxQuant software package, we identified 158 proteins in chicken egg white with two or more sequence unique peptides. This group of proteins identified with very high confidence included 79 proteins identified in egg white for the first time. In addition, 44 proteins were identified tentatively. CONCLUSIONS: Our results, apart from identifying many new egg white components, indicate that current mass spectrometry technology is sufficiently advanced to permit direct identification of minor components of proteomes dominated by a few major proteins without resorting to indirect techniques, such as chromatographic depletion or peptide library binding, which change the composition of the proteome. BioMed Central 2011-02-07 /pmc/articles/PMC3041730/ /pubmed/21299891 http://dx.doi.org/10.1186/1477-5956-9-7 Text en Copyright ©2011 Mann and Mann; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Mann, Karlheinz Mann, Matthias In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title | In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title_full | In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title_fullStr | In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title_full_unstemmed | In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title_short | In-depth analysis of the chicken egg white proteome using an LTQ Orbitrap Velos |
title_sort | in-depth analysis of the chicken egg white proteome using an ltq orbitrap velos |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041730/ https://www.ncbi.nlm.nih.gov/pubmed/21299891 http://dx.doi.org/10.1186/1477-5956-9-7 |
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