Relevant bibliographies by topics / Major Royal Jelly Proteins

Academic literature on the topic 'Major Royal Jelly Proteins'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Major Royal Jelly Proteins.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Major Royal Jelly Proteins"

1

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 text
Abstract:
Background: To date, there is no x-ray crystallography or structures from nuclear magnetic resonance (NMR) on royal jelly proteins available in the online data banks. In addition, characterization of proteins in royal jelly is not fully accomplished to date. Although new investigations unravel novel proteins in royal jelly, the majority of a protein family is present in high amounts (80-90%). Objective: In this review, we attempted to predict the three-dimensional structure of royal jelly proteins (especially the major royal jelly proteins) to allow visualization of the four protein surface properties (aromaticity, hydrophobicity, ionizability and (hydrogen (H)-bond) by using bioinformatics tools. Furthermore, we gathered the information on available therapeutic activities of crude royal jelly and its proteins. Methods: For protein modeling, prediction and analysis, the Phyre2 web portal systematically browsed in which the modeling mode was intensive. On the other side, to build visualized understanding of surface aromaticity, hydrophobicity, ionizability and H-bond of royal jelly proteins, the Discovery Studio 4.1 (Accelrys Software Inc.) was used. Results: Our in silico study confirmed that all proteins treasure these properties, including aromaticity, hydrophobicity, ionizability and (hydrogen (H)-bond. Another finding was that newly discovered proteins in royal jelly do not belong to the major royal jelly protein group. Conclusion: In conclusion, the three dimensional structure of royal jelly proteins along with its major characteristics were successfully elucidated in this review. Further studies are warranted to elucidate the detailed physiochemical properties and pharmacotherapeutics of royal jelly proteins.
APA, Harvard, Vancouver, ISO, and other styles
2

Park, 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 text
APA, Harvard, Vancouver, ISO, and other styles
3

Park, 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 text
APA, Harvard, Vancouver, ISO, and other styles
4

Albert, 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 text
APA, Harvard, Vancouver, ISO, and other styles
5

KOROŠEC, 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 text
Abstract:
Bee products are a natural source of nutrients and biologically active compounds, which may also be found on the lists of functional ingredients. In our diets, mainly honey is used and to a lesser extent bee pollen and royal jelly. Propolis and bee venom are mainly used in apitherapy due to their therapeutic properties. Regarding the basic nutrients, honey is primarily a source of sugars, while protein and fat contents are considerable in royal jelly and pollen, which also contains dietary fiber. Bee products also contain small amounts of bioactive compounds that have antioxidant, antimicrobial, anti-inflammatory and antiviral effects. Honey is characterized by, among others, phenolic compounds, royal jelly proteins, oligosaccharides. Royal jelly contains specific fatty acids, including 10-hydroxy-2-decenoic acid, bioactive peptides, major royal jelly proteins, and pollen contains various vitamins, phenolic compounds, amino acids, unsaturated fatty acids. However, further research and clinical studies are needed to evaluate the effectiveness of bee products and to raise consumer awareness of the importance of their consumption. Honey, bee pollen and royal jelly are natural foods, which due to their composition may help to achieve the recommended daily intake of basic nutrients, and may also serve as a source of important bioactive compounds, and therefore undoubtedly belong to a balanced diet.
APA, Harvard, Vancouver, ISO, and other styles
6

Oliveira, 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 text
Abstract:
Royal jelly is an essential substance for the development of bees from larval to adult stages. Studies have identified a group of key proteins in royal jelly, denominated major royal jelly proteins (MRJPs). The group currently consists of nine proteins (MRJP1–MRJP9), with MRJP1 being the most abundant and MRJP3 being used as a microsatellite marker for the selection of queens with a greater production of royal jelly. The diet of bees is mostly composed of proteins, and supplementing this intake to encourage a higher production of their primary product is important for producers. It is estimated that, by adding probiotic and prebiotic organisms to their diets, the benefits to bees will be even greater, both for their immune systems and primary responses to stress. Circumstances that are adverse compared to those of the natural habitat of bees eventually substantially interfere with bee behavior. Stress situations are modulated by proteins termed heat shock proteins (HSPs). Among these, HSP70 has been shown to exhibit abundance changes whenever bees experience unusual situations of stress. Thus, we sought to supplement A. mellifera bee colony diets with proteins and prebiotic and probiotic components, and to evaluate the expression levels of MRJP3 and HSP70 mRNAs using qRT-PCR. The results revealed that differences in the expression of MRJP3 can be attributed to the different types of feed offered. Significant differences were evident when comparing the expression levels of MRJP3 and HSP70, suggesting that protein supplementation with pre/probiotics promotes positive results in royal jelly synthesis carried out by honey bee nurses.
APA, Harvard, Vancouver, ISO, and other styles
7

Bilikova, 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 text
Abstract:
Until now, the properties of honey have been defined based exclusively on the content of plant components in the nectar of given plant. We showed that apalbumin1, the major royal jelly (RJ) protein, is an authentic and regular component of honey. Apalbumin1 and other RJ proteins and peptides are responsible for the immunostimulatory properties and antibiotic activity of honey. For the quantification of apalbumin1, an enzyme-linked immunosorbent assay (ELISA) was developed using polyclonal anti-apalbumin1 antibody. The method is suitable for honey authenticity determination; moreover it is useful for detection of the honey, honeybee pollen and RJ in products of medicine, pharmacy, cosmetics, and food industry, where presences of these honeybee products are declared. Results from the analysis for presence and amount of apalbumin1 in honeys will be used for high-throughput screening of honey samples over the world. On the basis of our experiments which show that royal jelly proteins are regular and physiologically active components of honey we propose to change the definition of honey (according to the EU Honey Directive 2001/110/EC) as follows: Honey is a natural sweet substance produced by honey bees from nectar of plants or from secretions of plants, or excretions of plant sucking insects, which honey bees collect, transform by combining with major royal jelly proteins and other specific substances of their own, deposit, dehydrate, store and leave in the honey comb to ripen and mature.
APA, Harvard, Vancouver, ISO, and other styles
8

Baitala, 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 text
APA, Harvard, Vancouver, ISO, and other styles
9

Winkler, 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 text
Abstract:
One of the first tasks of worker honey bees (Apis mellifera) during their lifetime is to feed the larval offspring. In brief, young workers (nurse bees) secrete a special food jelly that contains a large amount of unique major royal jelly proteins (MRJPs). The regulation of mrjp gene expression is not well understood, but the large upregulation in well-fed nurse bees suggests a tight repression until, or a massive induction upon, hatching of the adult worker bees. The lipoprotein vitellogenin, the synthesis of which is regulated by the two systemic hormones 20-hydroxyecdysone and juvenile hormone, is thought to be a precursor for the production of MRJPs. Thus, the regulation of mrjp expression by the said systemic hormones is likely. This study focusses on the role of 20-hydroxyecdysone by elucidating its effect on mrjp gene expression dynamics. Specifically, we tested whether 20-hydroxyecdysone displayed differential effects on various mrjps. We found that the expression of the mrjps (mrjp1–3) that were finally secreted in large amounts into the food jelly, in particular, were down regulated by 20-hydroxyecdysone treatment, with mrjp3 showing the highest repression value.
APA, Harvard, Vancouver, ISO, and other styles
10

Furusawa, 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 text
Abstract:
Apisin, a protein that is unique to royal jelly (RJ), is known to compose the greater part of the RJ proteins and to exist as a heterooligomer containing major royal jelly protein 1 and apisimin. However, few reports on the methods for quantifying apisin have been published. Thus, we attempted to quantify apisin using HPLC, a widely used analytical technique, as described below. Isoelectric precipitation and size-exclusion chromatography were used to obtain the purified protein, which was identified as apisin by SDS-PAGE and LC-MS analyses. The purified apisin was lyophilized and then used to generate a calibration curve to quantify apisin in RJ. The apisin content was fairly constant (i.e., 3.93 to 4.67 w/w%) in natural RJ. This study is the first to describe a simple, standardized method for quantifying apisin using HPLC and suggests that apisin can be used as a benchmark for future evaluations of RJ quality.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Major Royal Jelly Proteins"

1

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.

Full text
Abstract:
Dissertação (mestrado)—Universidade de Brasília, Instituto de Ciências Biológicas, Departamento de Biologia Celular, Pós-Graduação em Biologia Molecular, 2012.
Submitted by Albânia Cézar de Melo (albania@bce.unb.br) on 2013-01-17T14:01:33Z No. of bitstreams: 1 2012_HumbertoGonczarowskaJorge.pdf: 4182565 bytes, checksum: 32af60ccdfdd2ecfee93fbb6d0737438 (MD5)
Approved for entry into archive by Guimaraes Jacqueline(jacqueline.guimaraes@bce.unb.br) on 2013-01-24T13:04:36Z (GMT) No. of bitstreams: 1 2012_HumbertoGonczarowskaJorge.pdf: 4182565 bytes, checksum: 32af60ccdfdd2ecfee93fbb6d0737438 (MD5)
Made available in DSpace on 2013-01-24T13:04:36Z (GMT). No. of bitstreams: 1 2012_HumbertoGonczarowskaJorge.pdf: 4182565 bytes, checksum: 32af60ccdfdd2ecfee93fbb6d0737438 (MD5)
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.
APA, Harvard, Vancouver, ISO, and other styles
2

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.

Full text
Abstract:
Tese (doutorado)—Universidade de Brasília, Instituto de Ciências Biológicas, Departamento de Biologia Celular, Pós-Graduação em Biologia Molecular, 2017.
Submitted by Albânia Cézar de Melo (albania@bce.unb.br) on 2017-06-23T16:23:53Z No. of bitstreams: 1 2017_SamuelCoelhoMandacaru.pdf: 9292757 bytes, checksum: 1a53ba8cc877a93480f8a2d77b63ff6d (MD5)
Approved for entry into archive by Raquel Viana (raquelviana@bce.unb.br) on 2017-07-27T20:55:36Z (GMT) No. of bitstreams: 1 2017_SamuelCoelhoMandacaru.pdf: 9292757 bytes, checksum: 1a53ba8cc877a93480f8a2d77b63ff6d (MD5)
Made available in DSpace on 2017-07-27T20:55:36Z (GMT). No. of bitstreams: 1 2017_SamuelCoelhoMandacaru.pdf: 9292757 bytes, checksum: 1a53ba8cc877a93480f8a2d77b63ff6d (MD5) Previous issue date: 2017-07-27
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.
APA, Harvard, Vancouver, ISO, and other styles
3

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 text
APA, Harvard, Vancouver, ISO, and other styles

Books on the topic "Major Royal Jelly Proteins"

1

Roald, Dahl. Los mejores relatos de Roald Dahl. Madrid: Loqueleo, 2016.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Roald, Dahl. The Umbrella Man and Other Stories. New York, USA: Viking, 1998.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Roald, Dahl. The Great Automatic Grammatizator: And Other Stories. London: Puffin, 1997.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Roald, Dahl. Umbrella Man: And Other Stories. New York: Puffin Books, 2000.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Roald, Dahl. The Great Automatic Grammatizator and Other Stories. London: Penguin Group UK, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Roald, Dahl. The Great Automatic Grammatizator: And other stories. London, England: Viking, 1996.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Roald, Dahl. The Great Automatic Grammatizator. 7th ed. London: Puffin Books, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Roald, Dahl. Great Automatic Grammatizator: & Other Stories. London: Puffin, 2017.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Roald, 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 text
APA, Harvard, Vancouver, ISO, and other styles
10

Roald, Dahl. Umbrella Man and Other Stories. Rebound by Sagebrush, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Major Royal Jelly Proteins"

1

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 text
Abstract:
Larval feeds for different castes of honey bees include exclusively royal jelly from 4–9 days of development for the queen, and for worker larvae, royal jelly and worker jelly for 4-6 and 6–9 days respectively, whereas for drone larvae, royal jelly and a blended composite mixture of honey and pollen grain for 4-6 and 6–9 days respectively. For the queen, worker, and drone larvae, larval feeds include royal jelly and worker jelly for 4-6 and 6–9 days respectively. Royal jelly is a thick, creamy substance that is produced by the hypopharyngeal and mandibular glands of worker honey bees. Its primary components include water, hydrocarbons, proteins, lipids, minerals, vitamins, and a small amount of various types of polyphenols. Because the queen eats different larvae than the worker bees, this triggers a chain reaction of biochemical reactions, which ultimately leads to a high concentration of juvenile and ecdysone hormones being released. These hormones, in turn, regulate the expression of different genes in a sequential manner. Queen larvae have a variant proteomic that promotes the healthy development of the female reproductive system, which in turn leads to profound fertility and immune protection, as well as a longer life span for the queen.
APA, Harvard, Vancouver, ISO, and other styles
2

Meurig 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 text
Abstract:
The nature and mode of operation of the Davy-Faraday Research Laboratory (DFRL) and the Royal Institution (RI), within which it is located, are described. Together, they are part laboratory, part library, and part theatre where topics of scientific and cultural interest are presented to the general public, including children. W. H. Bragg, for two decades, from 1923 onwards, made it one of the world’s foremost research centres for the use of X-ray to study molecules of biological and other interest. His associates, especially Astbury, Bernal, and Kathleen Yardley (later Dame Kathleen Lonsdale), and others made major advances in elucidating the nature of a variety of the constituents of living matter, including hair, fingernails, horns, and other examples of proteins. This chapter contains a guide to the nature of proteinaceous and other examples of living matter and serves as an introduction to the total beginner in the study of structural biology and its importance.
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Major Royal Jelly Proteins"

1

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 text
APA, Harvard, Vancouver, ISO, and other styles
2

Ma, 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 text
APA, Harvard, Vancouver, ISO, and other styles
3

Frunze, 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 text
APA, Harvard, Vancouver, ISO, and other styles
4

Jiang, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Major Royal Jelly Proteins' for particular source types:
Journal articles Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography