Literatura académica sobre el tema "Major Royal Jelly Protein 1"

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Artículos de revistas sobre el tema "Major Royal Jelly Protein 1"

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Kashima, Yuri, Satoshi Kanematsu, Saori Asai, et al. "Identification of a Novel Hypocholesterolemic Protein, Major Royal Jelly Protein 1, Derived from Royal Jelly." PLoS ONE 9, no. 8 (2014): e105073. http://dx.doi.org/10.1371/journal.pone.0105073.

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YAMAGUCHI, Kikuji, Shaoyu HE, Zhengyue LI, et al. "Quantification of Major Royal Jelly Protein 1 in Fresh Royal Jelly by Indirect Enzyme-Linked Immunosorbent Assay." Bioscience, Biotechnology, and Biochemistry 77, no. 6 (2013): 1310–12. http://dx.doi.org/10.1271/bbb.130013.

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Wang, Xueyu, Jie Dong, Jiangtao Qiao, Gensheng Zhang, and Hongcheng Zhang. "Purification and characteristics of individual major royal jelly protein 1–3." Journal of Apicultural Research 59, no. 5 (2020): 1049–60. http://dx.doi.org/10.1080/00218839.2020.1761071.

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Moriyama, Takanori, Aimi Ito, Sumire Omote, Yuri Miura, and Hiroki Tsumoto. "Heat Resistant Characteristics of Major Royal Jelly Protein 1 (MRJP1) Oligomer." PLOS ONE 10, no. 5 (2015): e0119169. http://dx.doi.org/10.1371/journal.pone.0119169.

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Shen, Li-rong, Yi-ran Wang, Liang Zhai, et al. "Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody." Journal of Zhejiang University-SCIENCE B 16, no. 2 (2015): 155–66. http://dx.doi.org/10.1631/jzus.b1400223.

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Lin, Na, Si Chen, Hong Zhang, Junmin Li, and Linglin Fu. "Quantification of Major Royal Jelly Protein 1 in Fresh Royal Jelly by Ultraperformance Liquid Chromatography–Tandem Mass Spectrometry." Journal of Agricultural and Food Chemistry 66, no. 5 (2018): 1270–78. http://dx.doi.org/10.1021/acs.jafc.7b05698.

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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.

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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
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Tamura, Shougo, Shizuka Amano, Toru Kono, et al. "Molecular characteristics and physiological functions of major royal jelly protein 1 oligomer." PROTEOMICS 9, no. 24 (2009): 5534–43. http://dx.doi.org/10.1002/pmic.200900541.

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Ibarra-Herrera, Celeste C., Mario A. Torres-Acosta, Gonzalo I. Mendoza-Ochoa, Jose M. Aguilar-Yañez, and Marco Rito-Palomares. "Recovery of major royal jelly protein 1 expressed inPichia pastorisin aqueous two-phase systems." Journal of Chemical Technology & Biotechnology 89, no. 7 (2014): 941–47. http://dx.doi.org/10.1002/jctb.4342.

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Majtán, Juraj, Elena Kováčová, Katarína Bíliková та Jozef Šimúth. "The immunostimulatory effect of the recombinant apalbumin 1–major honeybee royal jelly protein–on TNFα release". International Immunopharmacology 6, № 2 (2006): 269–78. http://dx.doi.org/10.1016/j.intimp.2005.08.014.

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Tesis sobre el tema "Major Royal Jelly Protein 1"

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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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Dissertação (mestrado)—Universidade de Brasília, Instituto de Ciências Biológicas, Departamento de Biologia Celular, Pós-Graduação em Biologia Molecular, 2012.<br>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)<br>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: 32af60ccdfdd2ecfee93fbb6
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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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Tese (doutorado)—Universidade de Brasília, Instituto de Ciências Biológicas, Departamento de Biologia Celular, Pós-Graduação em Biologia Molecular, 2017.<br>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)<br>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)<br>Made available in DS
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Libros sobre el tema "Major Royal Jelly Protein 1"

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Rivett, DE, CW Ward, LM Belkin, JAM Ramshaw, and JFK Wilshire. Lennox Legacy. CSIRO Publishing, 1996. http://dx.doi.org/10.1071/9780643105072.

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The Lennox Legacy: The history of the CSIRO Laboratory at 343 Royal Parade Parkville records many of the events and incidents associated with the genesis and development of the Division of Protein Chemistry over a period of more than fifty years. This book has been titled in honour of Dr Francis Gordon Lennox, the Laboratory's founder and a man who believed that science has an important part to play in bettering the well-being of all Australians. His vision, over the years, of the critical importance of protein chemistry to Australian science and industry, was central to the Laboratory's natio
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Capítulos de libros sobre el tema "Major Royal Jelly Protein 1"

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Li, Jie Jack. "Blood Thinners: From Heparin to Plavix." In Blockbuster Drugs. Oxford University Press, 2014. http://dx.doi.org/10.1093/oso/9780199737680.003.0008.

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Three types of blood cells exist in the human body: red blood cells, white blood cells, and platelets, in addition to plasma, which takes up 55 percent of the blood’s volume. Red blood cells take up approximately 45 percent of the blood’s volume. They transport oxygen from the lungs to other body parts. White cells defend us against bacterial and viral invasions. Platelets (less than 1 percent of the blood), the third type of blood cells, are sticky little cell fragments that are involved in helping the blood clot, a process known as coagulation. Without platelets (even though they constitute less than 1 percent of blood), our blood would not be able to clot, and we would have uncontrolled bleeding. However, formation of blood clots is a double-edged sword. Clots are beneficial because they heal cuts and wounds; blood clots in the bloodstream are harmful because they block coronary arteries, constrict vital oxygen supplies, and cause heart attacks and strokes, more and more frequent modern maladies as the baby boomers get older. Whenever the body is cut or injured and blood comes into contact with cells outside the bloodstream, a tissue factor on these cells encounters a particular protein within the blood, which triggers the clotting process. In the same vein, a series of other blood factors then come into action and amplify one another to quickly form a jelly-like blood clot. Blood clots form when an enzyme called thrombin marshals fibrin (a blood protein) and platelets (tiny cells that circulate in the blood) to coagulate at the site of an injury. Individuals with no ability to clot have a genetic condition called hemophilia; such people are also known as “bleeders.” Queen Victoria was hemophilic, and she passed on her genes to her many heirs who ruled Europe for over a century. This is why hemophilia is sometimes known as the royal disease. Symptoms of hemophilia manifest only in male offspring. People with hemophilia must periodically administer a clotting factor to their blood to prevent constant bleeding.
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Actas de conferencias sobre el tema "Major Royal Jelly Protein 1"

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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.

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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.

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