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Profiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nurse-honeybees (Apis mellifera L.)

dc.contributor.authorSantos, K. S.
dc.contributor.authordos Santos, L. D.
dc.contributor.authorMendes, M. A.
dc.contributor.authorde Souza, B. M.
dc.contributor.authorMalaspina, O.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:55:37Z
dc.date.available2014-05-20T13:55:37Z
dc.date.issued2005-01-01
dc.description.abstractThe protein complement of the secretion from hypopharyngeal gland of nurse-bees (Apis mellifera L.) was partially identified by using a combination of 2D-PAGE, peptide sequencing by MALDI-PSD/MS and a protein engine identification tool applied to the honeybee genome. The proteins identified were compared to those proteins already identified in the proteome complement of the royal jelly of the honey bees. The 2D gel electrophoresis demonstrated this protein complement is constituted of 61 different polypepides, from which 34 were identified as follows: 27 proteins belonged to MRJPs family, 5 proteins were related to the metabolism of carbohydrates and to the oxido-reduction metabolism of energetic Substrates, I protein was related to the accumulation of iron in honeybee bodies and I protein may be a regulator of MRJP-1 oligomerization. The proteins directly involved with the carbohydrates and energetic metabolisms were: alpha glucosidase, glucose oxidase and alpha amylase, whose are members of the same family of enzymes, catalyzing the hydrolysis of the glucosidic linkages of starch; alcohol dehydrogenase and aldehyde dehydrogenase, whose are constituents of the energetic metabolism. The results of the present manuscript support the hypothesis that the most of these proteins are produced in the hypoharyngeal gland of nurse-bees and secreted into the RJ. (C) 2004 Elsevier Ltd. All rights reserved.en
dc.description.affiliationUniv São Paulo, UNESP, Ctr Study Soc Insects, CEIS,Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationUnespUniv São Paulo, UNESP, Ctr Study Soc Insects, CEIS,Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.format.extent85-91
dc.identifierhttp://dx.doi.org/10.1016/j.ibmb.2004.10.003
dc.identifier.citationInsect Biochemistry and Molecular Biology. Oxford: Pergamon-Elsevier B.V., v. 35, n. 1, p. 85-91, 2005.
dc.identifier.doi10.1016/j.ibmb.2004.10.003
dc.identifier.issn0965-1748
dc.identifier.lattes7538556085505819
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19912
dc.identifier.wosWOS:000226402700009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInsect Biochemistry and Molecular Biology
dc.relation.ispartofjcr3.562
dc.relation.ispartofsjr1,912
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectAfricanized Apis melliferapt
dc.subjectroyal jellypt
dc.subjectpeptide mass fingerprintspt
dc.subjectproteomept
dc.subjectMALDI-TOFpt
dc.titleProfiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nurse-honeybees (Apis mellifera L.)en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes7538556085505819
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-1650-257X[5]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Rio Claropt
unesp.departmentBiologia - IBpt

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