Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/66998
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: Can museum egg specimens be used for proteomic analyses?
Author: Portugal, S.
Cooper, H.
Zampronio, C.
Wallace, L.
Cassey, P.
Citation: Proteome Science, 2010; 8(1):40-44
Publisher: BioMed Central Ltd.
Issue Date: 2010
ISSN: 1477-5956
1477-5956
Statement of
Responsibility: 
Steven J Portugal, Helen J Cooper, Cleidiane G Zampronio, Laine L Wallace, Phillip Cassey
Abstract: Background: Mass spectrometry and proteomic analyses have become powerful tools for the analysis of proteins and peptides. Investigation of proteins contained in the various layers of the avian eggshell has focused entirely on domesticated species. It has been widely assumed that this existing research can inform the study of wild bird species despite the fact that the vast majority of the diversity in avian species (~95%) exists outside the Orders to which domestic and poultry species belong. Museum collections offer a potentially valuable source of material for studying composition of wild avian eggshell matrix proteins. We used museum and fresh eggshells of common quails Coturnix coturnix to compare the protein composition of their organic matrices. Four eggs of domestic chickens were analysed simultaneously as a control for comparison to the fresh and museum quail eggs. The determination of the proteins was carried out using enzymatic cleavage followed by high-performance mass spectrometry. Results: We found that some of the expected key eggshell proteins (3 out of 11) were not present in the samples of museum quail egg. These proteins were either entirely absent from the museum eggs or the technique was unable to detect them. There was no pattern in the absent proteins in the sense of protein function or where they are located within the eggshell. Conclusion: We conclude it is likely that such studies on museum specimens using a proteomic approach will be limited in coverage of proteins and may, therefore, be misleading.
Description: Extent: 5p.
Rights: © 2010 Portugal et al; licensee BioMed Central Ltd. 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.
RMID: 0020112288
DOI: 10.1186/1477-5956-8-40
Published version: http://www.proteomesci.com/content/8/1/40
Appears in Collections:Earth and Environmental Sciences publications
Environment Institute Leaders publications

Files in This Item:
File Description SizeFormat 
hdl_66998.pdfPublished version288.57 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.