Academic literature on the topic 'Major Royal Jelly Proteins'
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Journal articles on the topic "Major Royal Jelly Proteins"
Hossen, Md Sakib, Taebun Nahar, Siew Hua Gan, and Md Ibrahim Khalil. "Bioinformatics and Therapeutic Insights on Proteins in Royal Jelly." Current Proteomics 16, no. 2 (January 4, 2019): 84–101. http://dx.doi.org/10.2174/1570164615666181012113130.
Full textPark, Min Ji, Bo Yeon Kim, Yijie Deng, Hee Geun Park, Yong Soo Choi, Kwang Sik Lee, and Byung Rae Jin. "Antioxidant capacity of major royal jelly proteins of honeybee (Apis mellifera) royal jelly." Journal of Asia-Pacific Entomology 23, no. 2 (June 2020): 445–48. http://dx.doi.org/10.1016/j.aspen.2020.03.007.
Full textPark, Hee Geun, Bo Yeon Kim, Min Ji Park, Yijie Deng, Yong Soo Choi, Kwang Sik Lee, and Byung Rae Jin. "Antibacterial activity of major royal jelly proteins of the honeybee (Apis mellifera) royal jelly." Journal of Asia-Pacific Entomology 22, no. 3 (September 2019): 737–41. http://dx.doi.org/10.1016/j.aspen.2019.06.005.
Full textAlbert, Stefan, Debashish Bhattacharya, Jaroslav Klaudiny, Jana Schmitzová, and Jozef Simúth. "The Family of Major Royal Jelly Proteins and Its Evolution." Journal of Molecular Evolution 49, no. 2 (August 1999): 290–97. http://dx.doi.org/10.1007/pl00006551.
Full textKOROŠEC, Mojca, and Jasna BERTONCELJ. "Pomen čebeljih pridelkov v humani prehrani." Acta agriculturae Slovenica 115, no. 2 (June 1, 2020): 223. http://dx.doi.org/10.14720/aas.2020.115.2.632.
Full textOliveira, Maria Carolina Paleari Varjão, Eloisa Magalhaes Pereira, Maria Josiane Sereia, Érica Gomes Lima, Breno Gabriel Silva, Vagner Alencar Arnaut Toledo, and Maria Claudia Colla Ruvolo-Takasusuki. "Expression of MRJP3 and HSP70 mRNA Levels in Apis mellifera L. Workers after Dietary Supplementation with Proteins, Prebiotics, and Probiotics." Insects 13, no. 7 (June 24, 2022): 571. http://dx.doi.org/10.3390/insects13070571.
Full textBilikova, Katarina, Tatiana Kristof Krakova, Kikuji Yamaguchi, and Yoshihisa Yamaguchi. "Major royal jelly proteins as markers of authenticity and quality of honey / Glavni proteini matične mliječi kao markeri izvornosti i kakvoće meda." Archives of Industrial Hygiene and Toxicology 66, no. 4 (December 1, 2015): 259–67. http://dx.doi.org/10.1515/aiht-2015-66-2653.
Full textBaitala, Tatiane Vicente, Patrícia Faquinello, Vagner de Alencar Arnaut de Toledo, Claudete Aparecida Mangolin, Elias Nunes Martins, and Maria Claudia Colla Ruvolo-Takasusuki. "Potential use of major royal jelly proteins (MRJPs) as molecular markers for royal jelly production in Africanized honeybee colonies." Apidologie 41, no. 2 (November 27, 2009): 160–68. http://dx.doi.org/10.1051/apido/2009069.
Full textWinkler, Paul, Frank Sieg, and Anja Buttstedt. "Transcriptional Control of Honey Bee (Apis mellifera) Major Royal Jelly Proteins by 20-Hydroxyecdysone." Insects 9, no. 3 (September 19, 2018): 122. http://dx.doi.org/10.3390/insects9030122.
Full textFurusawa, Takako, Yasuko Arai, Kenji Kato, and Kenji Ichihara. "Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly." Evidence-Based Complementary and Alternative Medicine 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/5040528.
Full textDissertations / Theses on the topic "Major Royal Jelly Proteins"
Jorge, Humberto Gonczarowska. "Análise de associações de major royal jelly protein 1 por cromatografia de exclusão molecular." reponame:Repositório Institucional da UnB, 2012. http://repositorio.unb.br/handle/10482/11959.
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Polifenismo é a habilidade de um genoma expressar múltiplos fenótipos morfológica e comportamentalmente distintos. Em abelhas Apis mellifera¸ o polifenismo é essencial, uma vez que gera divisão de tarefas na colméia, vital para sua viabilidade. A plasticidade fenotípica das abelhas é mediada nutricionalmente pela geleia real (GR). A major royal jelly protein 1 (MRJP1) é a mais abundante proteína da GR, e é descrita como o principal fator ativo na diferenciação de castas de Apis mellifera. A MRJP1 é uma glicoproteína que se liga fortemente a um peptídeo chamado apisimina (5,5 kDa) e se auto-associa, formando complexos de diferentes tamanhos, podendo se apresentar em diversas formas moleculares numa única solução. O objetivo deste trabalho foi caracterizar associações de MRPJ1 sob diversas condições. MRJP1 foi purificada em um único passo de cromatografia de troca iônica. Por cromatografia de exclusão molecular foi possível observar que a MRJP1 tende a se oligomerizar ou até mesmo a se agregar em tampões ácidos, em amostras aquecidas a 60ºC ou em tampões com alta molaridade de sal (2 M de NaCl) ou de glicina (2 M),. Em tampão PBS pH neutro e tampão carbonato/bicarbonato pH 10,0, a MRJP1 está presente em três formas -pentâmero (290 kDa), dímero (120 kDa) e monômero (55 kDa). Ao se adicionar 0,5 M de glicina em tampão carbonato/bicarbonato pH 10,0, a MRJP1 se dissocia, apresentando-se mais abundante nas formas dimérica e monomérica. A presença dos surfactantes dodecil sulfato de sódio, Tween® 20 e Brij 35 induz um aumento na massa dos complexos de MRJP1, causado provavelmente pela ligação de moléculas do detergente com a proteína, podendo também induzir oligomerização ou agregação. Logo, conclui-se que a liofilização e aquecimento das amostras de MRJP1 induzem oligomerização e agregação da amostra. Não liofilizar o monômero e mantê-lo em baixas temperaturas mantém a amostra nesta forma molcular. O tampão carbonato/bicarbonato, pH 10,0, contendo glicina 0,5 M foi o melhor para se obter menor quantidade de formas de MRJP1 em solução com grande quantidade de monômero. O processo de ultrafiltração impede a purificação de MRJP1 em cromatografia de troca-iônica. ______________________________________________________________________________ ABSTRACT
Polyphenism is the hability of a genome to express multiple phenotypes with different morphologies and behaviors. In Apis mellifera bees, the polyphenism is essential, once it generates labor division in the hive, vital to its viability. The bee s phenotypic plasticity is nutritionally mediated by royal jelly (GR). The major royal jelly protein 1 (MRJP1) is the most abundant protein in GR, and it is described as the main active factor in differentiating Apis mellifera castes. The MRJP1 is a glycoprotein that binds strongly to a peptide named apsimin (5,5 kDa) and self-associates, forming complexes of various sizes, and may present itself in different molecular forms in one solution. The purpose of this study was to characterize MRJP1 associations under different conditions. MRJP1 was purified in a single step of ionic exchange chromatography. By size exclusion chromatography, it was possible to observe the MRJP1 oligomerization or even aggregation in acid buffers, in samples heated to 60ºC or in buffers with high salt molarity (2 M of NaCl) or glycine (2 M). In PBS buffer at neutral pH and carbonate/bicarbonate pH 10,0 buffer, MRJP1 was present in three forms - pentamer (290 kDa), dimer (120 kDa) or monomer (55 kDa). By adding 0.5 M of glycine in carbonate/bicarbonate pH 10,0 buffer, MRJP1 dissociates, leading to monomer and dimmer as the most abundant forms. The presence of the surfactants sodium dodecyl sulfate, Tween® 20 and Brij 35 induces a mass increase in the MRJP1 complex, probably caused by the binding of detergent molecules to the protein. Detergents may also induce oligomerization or aggregation. Therefore, it is concluded that lyophilization and heating the MRJP1 samples induce oligomerization and aggregation of the sample. To not lyophilize the monomer and keep it at low temperatures maintains the sample in this molecular form. The carbonate/bicarbonate buffer, pH 10.0, containing 0.5 M of glycine was the best for obtaining fewer MRJP1 forms in solution with high amounts of monomer. The ultrafiltration process prevents MRJP1 purification by ion exchange chromatography.
Mandacaru, Samuel Coelho. "Estrutura oligomérica e dinâmica de Major Royal Jelly Protein 1 (MRJP1)/apisimina analisadas por espectrometria de massas e técnicas complementares." reponame:Repositório Institucional da UnB, 2017. http://repositorio.unb.br/handle/10482/23924.
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Geleia Real (GR) dispara o desenvolvimento de larvas de abelhas fêmeas até rainhas. Este efeito tem sido atribuído à presença de Major Royal Jelly Protein 1 (MRJP1) presente na geleia real. MRJP1 isolada de GR está intimamente associada a apisimina, um peptídeo helicoidal com 54 resíduos de aminoácidos que promove uma associação não covalente de MRJP1 em oligômeros de diferentes tamanhos. Não existem dados de alta resolução disponíveis para essas estruturas e até mesmo sua estequiometria ainda não é clara. Nesta tese, examinamos a relação MRJP1/apisimina usando um arsenal de técnicas biofísicas. Também, investigamos o comportamento de MRJP1/apisimina em amostras após remoção de seus carboidratos e de apisimina associada. Nossos dados de espectrometria de massas (MS) nativos demonstraram que os complexos existem predominantemente numa estequiometria de MRJP14/apisimina4. Blue native PAGE demonstrou a prevalência de estruturas tetraméricas e monoméricas. Microscopia de força atômica demonstrou a presença de populações que puderam ser agrupadas em dois grandes grupos. Troca do hidrogênio por deutério (HDX) seguida de análises por espectrometria de massas revelaram que MRJP1, nesses complexos, é desordenada na extensão dos resíduos 20-265. Estruturas secundárias (provavelmente folhas beta antiparalelas) estáveis são encontradas marginalmente ao redor dos resíduos 266-432. Estas são regiões fracamente estruturadas com conformações que variam entre estruturada e desestruturada, gerando uma distribuição isotópica bimodal (EX1). Nós propomos que os complexos nativos (tetrâmeros) têm uma estrutura quaternária formada por “dímero de dímero”, onde as cadeias de MRJP1 são ligadas por apisimina. Especificamente, nossos dados sugerem que apisimina age como um ligante que forma contatos hidrofóbicos envolvendo o segmento 316VLFFGLV322 de MRJP1. Esta proteína tem dois sítios de glicosilação localizados nos resíduos de aminoácidos 144 e 177. Por 2DE podemos ver 9 proteoformas de MRJP1, mesmo após a remoção dos carboidratos. Deglicosilação produz grandes agregados solúveis, enfatizando o papel dos glicanos como inibidores de agregação. Amostras com apisimina parcialmente removida formam complexos diméricos com estequiometria (MRJP12/apisimina1). As informações produzidas neste trabalho podem contribuir para uma melhor compreensão da relação estrutura/função de MRJP1, que possui papéis únicos na biologia da abelha.
Royal jelly (RJ) triggers the development of female honeybee larvae into queens. This effect has been attributed to the presence of major royal jelly protein 1 (MRJP1) in RJ. MRJP1 isolated from royal jelly is tightly associated with apisimin, a 54-residue -helical peptide that promotes the noncovalent assembly of MRJP1 into multimers. No high resolution structural data are available for these complexes, and their binding stoichiometry remains uncertain. We examined MRJP1/apisimin using a range of biophysical techniques. In addition, we investigated the behavior of deglycosylated samples, as well as samples with reduced apisimin content. Our mass spectrometry (MS) data demonstrated that the native complexes predominantly exist in a (MRJP14 apisimin4) stoichiometry. Blue native and showed the prevalence of tetrameric and monomeric structures in native conditions. Atomic force microscopy also showed two populations. Hydrogen/deuterium exchange (HDX) MS revealed that MRJP1 within these complexes is extensively disordered in the range of the residues 20-265. Marginally stable secondary structure (likely antiparallel -sheet) exists around residues 266-432. These weakly structured regions interchange with conformations that are extensively unfolded, giving rise to bimodal (EX1) isotope distributions. We propose that the native complexes have a “dimer of dimers” quaternary structure in which MRJP1 chains are bridged by apisimin. Specifically, our data suggest that apisimin acts as a linker that forms hydrophobic contacts involving the MRJP1 segment 316VLFFGLV322. MRJP1 has 2 glycosites located at amino acids 144 and 177. By using 2-DE, we observed 9 MRJP1 proteoforms, even after carbohydrate removal. Deglycosylation produces large soluble aggregates, highlighting the role of glycans as aggregation inhibitors. Samples with reduced apisimin content form dimeric complexes with a (MRJP12 apisimin1) stoichiometry. Therefore, the information uncovered in this work should help pave the way towards a better understanding of the structure/function relationship for MRJP1, which possesses unique roles in the honey bee biology.
Wu, Tz-Shian, and 吳姿嫺. "Usage of anion exchange chromatography to purify major proteins in the pericarp of jelly fig (Ficus awkeotsang Makino) achenes." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/t99nea.
Full textBooks on the topic "Major Royal Jelly Proteins"
Roald, Dahl. Los mejores relatos de Roald Dahl. Madrid: Loqueleo, 2016.
Find full textRoald, Dahl. The Umbrella Man and Other Stories. New York, USA: Viking, 1998.
Find full textRoald, Dahl. The Great Automatic Grammatizator: And Other Stories. London: Puffin, 1997.
Find full textRoald, Dahl. Umbrella Man: And Other Stories. New York: Puffin Books, 2000.
Find full textRoald, Dahl. The Great Automatic Grammatizator and Other Stories. London: Penguin Group UK, 2009.
Find full textRoald, Dahl. The Great Automatic Grammatizator: And other stories. London, England: Viking, 1996.
Find full textRoald, Dahl. The Great Automatic Grammatizator. 7th ed. London: Puffin Books, 2001.
Find full textRoald, Dahl. Great Automatic Grammatizator: & Other Stories. London: Puffin, 2017.
Find full textRoald, Dahl. The Umbrella Man and Other Stories : L'Homme au Parapluie et Autres Nouvelles (Bilingual FRench and English edition). French & European Pubns, 2003.
Find full textRoald, Dahl. Umbrella Man and Other Stories. Rebound by Sagebrush, 2001.
Find full textBook chapters on the topic "Major Royal Jelly Proteins"
Marwaha, Lovleen. "Royal Jelly as Larval Food for Honey Bees." In The Polyandrous Queen Honey Bee: Biology and Apiculture, 67–82. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815079128112010005.
Full textMeurig Thomas, John. "W. H. Bragg and His Creation of a World-Famous Centre for X-ray Crystallography at the Davy-Faraday Research Laboratory." In Architects of Structural Biology, 41–73. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780198854500.003.0003.
Full textConference papers on the topic "Major Royal Jelly Proteins"
Buttstedt, Anja. "Characterization of major royal jelly protein 1 and 2 of the western honey beeApis mellifera." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.110376.
Full textMa, Xin, Shubao Yang, Wei Jin, Yunjiao Zhao, Hongxia Ma, and Weimin Luan. "Construction of a Recombinant Major Royal Jelly Protein 1 (MRJP1) Expression Vector for Mammary Gland-Specific Expression." In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.114.
Full textFrunze, O., Y. S. Choi, H. G. Park, and E. J. Kang. "FEATURES OF SOLUBLE PROTEINS ROYAL JELLY APIS MELLIFERA L. DEPENDING ON TEMPERATURE." In Современные проблемы пчеловодства и апитерапии. Рыбное: Федеральное государственное бюджетное научное учреждение "Федеральный научный центр пчеловодства", 2021. http://dx.doi.org/10.51759/pchel_api_2021_295.
Full textJiang, Jian-Hui, Jian-Bo Zhao, Hui-Ping Ding, Wen-Bo Xin, and Long Chen. "The Antioxidant Activity of Royal Jelly Water Soluble Proteins Hydrolysate from Xinjiang Black Bee." In 2017 2nd International Conference on Biological Sciences and Technology (BST 2017). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/bst-17.2018.34.
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