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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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Detalles Bibliográficos
Autores principales: Mann, Karlheinz, Mann, Matthias
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
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.
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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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