Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva

Detalhes bibliográficos
Autor(a) principal: Lamy, E.
Data de Publicação: 2008
Outros Autores: da Costa, G., Capela e Silva, Fernando, Potes, J.C., Coelho, A.V., Sales Baptista, E.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10174/1543
Resumo: Saliva provides a medium for short-term adaptation to changes in diet composition, namely, the presence of plant secondary metabolites. Salivary proteins have biological functions that have particular influence on oral homeostasis, taste, and digestive function. Some salivary proteins, such as proline-rich proteins, are present in browsers but absent in grazers. Despite the significance of salivary proteins, their expression patterns in many herbivores are unknown. We investigated the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile of parotid salivary proteins from two domesticated species, one a grazer, the sheep, Ovis aries, and the other a mixed feeder, the goat, Capra hircus, both fed on the same conventional diet. With 12.5% polyacrylamide linear gels, we observed uniform patterns of salivary proteins within the two species. In the goat profile, 21 major bands were observed, and 19 in the sheep profile. Each band was subjected to peptide mass fingerprinting for purposes of identification, allowing for 16 successful protein identifications. Marked differences were observed between the species in the region of 25–35 kDa molecular weights: one band was present in significantly different intensities; three bands were present only in goats; and one band was present only in sheep. This is the first report of a comparison of the protein salivary composition of sheep and goats and suggests that future research should be conducted to reveal a physiological function for salivary proteins related to the differences in feeding behavior of these species.
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spelling Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid SalivaCapra hircusFeeding behaviorMALDI-TOFMSOvis ariesParotid salivaProtein identificationSalivary proteinsSDS-PAGESaliva provides a medium for short-term adaptation to changes in diet composition, namely, the presence of plant secondary metabolites. Salivary proteins have biological functions that have particular influence on oral homeostasis, taste, and digestive function. Some salivary proteins, such as proline-rich proteins, are present in browsers but absent in grazers. Despite the significance of salivary proteins, their expression patterns in many herbivores are unknown. We investigated the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile of parotid salivary proteins from two domesticated species, one a grazer, the sheep, Ovis aries, and the other a mixed feeder, the goat, Capra hircus, both fed on the same conventional diet. With 12.5% polyacrylamide linear gels, we observed uniform patterns of salivary proteins within the two species. In the goat profile, 21 major bands were observed, and 19 in the sheep profile. Each band was subjected to peptide mass fingerprinting for purposes of identification, allowing for 16 successful protein identifications. Marked differences were observed between the species in the region of 25–35 kDa molecular weights: one band was present in significantly different intensities; three bands were present only in goats; and one band was present only in sheep. This is the first report of a comparison of the protein salivary composition of sheep and goats and suggests that future research should be conducted to reveal a physiological function for salivary proteins related to the differences in feeding behavior of these species.2009-04-15T10:02:32Z2009-04-152008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article51004 bytesapplication/pdfhttp://hdl.handle.net/10174/1543http://hdl.handle.net/10174/1543eng388-397Journal of Chemical Ecology334livrendndfcs@uevora.ptndndnd226Lamy, E.da Costa, G.Capela e Silva, FernandoPotes, J.C.Coelho, A.V.Sales Baptista, E.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-01-03T18:37:14Zoai:dspace.uevora.pt:10174/1543Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:57:25.189355Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
title Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
spellingShingle Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
Lamy, E.
Capra hircus
Feeding behavior
MALDI-TOFMS
Ovis aries
Parotid saliva
Protein identification
Salivary proteins
SDS-PAGE
title_short Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
title_full Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
title_fullStr Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
title_full_unstemmed Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
title_sort Comparison of Electrophoretic Protein Profiles from Sheep and Goat Parotid Saliva
author Lamy, E.
author_facet Lamy, E.
da Costa, G.
Capela e Silva, Fernando
Potes, J.C.
Coelho, A.V.
Sales Baptista, E.
author_role author
author2 da Costa, G.
Capela e Silva, Fernando
Potes, J.C.
Coelho, A.V.
Sales Baptista, E.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Lamy, E.
da Costa, G.
Capela e Silva, Fernando
Potes, J.C.
Coelho, A.V.
Sales Baptista, E.
dc.subject.por.fl_str_mv Capra hircus
Feeding behavior
MALDI-TOFMS
Ovis aries
Parotid saliva
Protein identification
Salivary proteins
SDS-PAGE
topic Capra hircus
Feeding behavior
MALDI-TOFMS
Ovis aries
Parotid saliva
Protein identification
Salivary proteins
SDS-PAGE
description Saliva provides a medium for short-term adaptation to changes in diet composition, namely, the presence of plant secondary metabolites. Salivary proteins have biological functions that have particular influence on oral homeostasis, taste, and digestive function. Some salivary proteins, such as proline-rich proteins, are present in browsers but absent in grazers. Despite the significance of salivary proteins, their expression patterns in many herbivores are unknown. We investigated the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile of parotid salivary proteins from two domesticated species, one a grazer, the sheep, Ovis aries, and the other a mixed feeder, the goat, Capra hircus, both fed on the same conventional diet. With 12.5% polyacrylamide linear gels, we observed uniform patterns of salivary proteins within the two species. In the goat profile, 21 major bands were observed, and 19 in the sheep profile. Each band was subjected to peptide mass fingerprinting for purposes of identification, allowing for 16 successful protein identifications. Marked differences were observed between the species in the region of 25–35 kDa molecular weights: one band was present in significantly different intensities; three bands were present only in goats; and one band was present only in sheep. This is the first report of a comparison of the protein salivary composition of sheep and goats and suggests that future research should be conducted to reveal a physiological function for salivary proteins related to the differences in feeding behavior of these species.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-01T00:00:00Z
2009-04-15T10:02:32Z
2009-04-15
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10174/1543
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dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 388-397
Journal of Chemical Ecology
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