Identificação das glicoproteínas da geléia real de Apis mellifera L. por análise em MALDI-TOF MS

• Ano de defesa: 2007
• Autor(a) principal: Teixeira, Renata Roland
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Uberlândia; BR; Programa de Pós-graduação em Genética e Bioquímica; Ciências Biológicas; UFU
• Palavras-chave em Português: Apalbumina; Abelha; Proteoma; Concanavalina A; Geléia real; Proteínas; MRJP; Apalbumin; Honeybee; Proteom; Royal jelly; CNPQ::CIENCIAS BIOLOGICAS::GENETICA
• Link de acesso: https://repositorio.ufu.br/handle/123456789/15902

The royal jelly (RJ), a secretion produced by the hipopharingeal and mandibular glands of the nurse honeybees, have a variety of pharmacological activities, aside of being necessary for the castes differentiation and the queen Apis mellifera longevity. To identify the N-glycoproteins of two samples of RJ provinient from distinct origin and conditions, we used the concanavalin A affinity chromatography (ConA) associated to the mass spectrometry. The investigated samples of RJ were the brazilian RJ (GRB), produced experimentally in local apiary, and the Chinese RJ (GRC), mattered from China and commercially available. The protein profile in SDS-PAGE 1D was characteristic for GRB and GRC. The N-glycoproteins fractions eluted from the ConA column had presented nine polypeptides for GRB and 12 for GRC, with relative molecular mass (Mr) varying between 130 and 15 kDa. It was observed that the immediately aftercollects freezing of the GRB did not inhibited the appearance of bands with Mr lesser than 49 kDa. A total of 21 bands was excised from gel and digested with tripisin for analysis in MALDI-TOF MS. The bioinformatic analysis revealed that all the 16 proteins identified in the GRB and GRC samples belong to the A. mellifera apalbumins family (Apa-1, Apa-2 and Apa-3). The Apa-2 was the protein that had greater prevalence between the N-glycoproteins of the RJ, presenting Mr varying between 110 and 25 kDa. The fact that the Apa-2 had been identified with distinct Mrs can be related to glycosilation, oligomerization or degradation of this apalbumin. Therefore, the ConA affinity chromatography associated with the proteomic analysis made possible the identification of three members of the family of RJ main proteins (Apa-1, Apa-2 and Apa-3). Moreover, the comparative study of the GRB and GRC glycoprotein composition suggests similar standard between these samples and can be useful in future studies that evaluate the biological functions of the apalbumins pos-translational modifications.