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Nonvolatile Thin Film Transistor Memory with Ferritin
Kazunori Ichikawa,Mami Fujii,Prakaipetch Punchaipetch,Hiroshi Yano,Tomoaki Hatayama,Takashi Fuyuki,Ichiro Yamashita,Yukiharu Uraoka 한국물리학회 2009 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.54 No.1
The low-temperature polycrystalline silicon (poly-Si) thin film transistor (LTPS-TFT) flash memory is a potential candidate as a key component of the system on panel (SOP). We have proposed the “bio-nano-process” for the fabrication of nanodots by using biotechnology. In this study, we have successfully fabricated and developed a LTPS-TFT flash memory with biomineralized inorganic nanodots for the first time. High-density homogeneous nanodots were made to adsorb on a silicon film by using ferritin protein without the use of vacuum systems at high temperature. Electron charging and discharging in the dots were clearly confirmed from the transient behavior of the transfer curve at room temperature. This fabrication technique is promising for the development of a flash memory for a SOP.
Jianping Chen,Jian Xu,Masato Hino,Mami Yamashita,Kazuma Hirata,Anandrao Ashok Patil,Tsuneyuki Tatsuke,Hiroaki Mon,Yutaka Banno,Takahiro Kusakabe,Jae Man Lee 한국응용곤충학회 2016 Journal of Asia-Pacific Entomology Vol.19 No.3
G protein-coupled receptors (GPCRs) are seven transmembrane proteins, which play an essential role in transmitting various extracellular signals into cells. For functional and structural analysis of GPCRs, it is necessary to produce active GPCRs in high quantitieswith outstanding purity. Fortunately, earlier baculovirus expression vector system has been reported as a proven functional GPCR mass-production tool. Therefore, in this study, we selected Bombyx mori allatostatin-C neuropeptide receptor BNGR-A1 as a GPCR reporter protein, which has been already proved successful binding of ligand. We confirmed its expression profile in various silkworm tissues and cell lines and then verified its plasma membrane subcellular localization in cultured silkworm BmN4 cells. In addition, we constructed recombinant baculoviruses for BNGR-A1, its ligand allatostatin-C (BmAST-C) and related eightG proteins (Gs, G12,Gα4, Gq, Gβ2,Gβ3, Gβ5 andGγ) and subsequentlymonitored the extracellular or intracellular expression of BNGR-A1 by co-infection with its ligand and cognate G proteins-expressing viruses. It is interesting to observe that different combinations of G proteins could result in changes or even undetectable of final yields of BNGR-A1, suggesting the essential roles of G proteins involved in the GPCR expression or stabilization. The present study demonstrated that co-infection of recombinant viruses expressing Gα4β3γ trimer enhanced the production of BNGR-A1 on BV fractions. To our knowledge, this is a fine strategy for identifying the specific G protein partner responsible for certain GPCR of interest. These studies would provide a novel idea for improving GPCR expression in the silkworm by baculovirus expression vector system.
Daisuke Morokuma,Jian Xu,Hiroaki Mon,Kazuma Hirata,Masato Hino,Shoko Kuboe,Mami Yamashita,Takahiro Kusakabe,이재만 한국응용곤충학회 2015 Journal of Asia-Pacific Entomology Vol.18 No.2
Glycosylation is an important post-translational modification that confers various biological activities, structural stability, and inter-molecular interactions to proteins. Baculovirus expression vector system (BEVS) is widely used to produce recombinant glycoproteins, which may not be suitable for clinical use due to differences in the N-linked glycan structure between insects and mammals. It is necessary to develop an appropriate model protein-base platform for glycoanalysis to engineer the insect-type N-glycosylation pathway into human type efficiently. In this study,we employed human plasma protein alpha 1-acid glycoprotein (α1AGP). Itwas highly secreted from cultured silkworm cells and larvae when using the BEVS and glycosylated with insect type N-linked glycans. Interestingly, when separated on SDS-PAGE, the purified recombinant α1AGP secreted into silkworm haemolymph generated six distinct products from three alternative translates, suggesting that α1AGP has variations for the recognition or choice of glycosylation sites.
Masato Hino,Takuji Kawanami,Jian Xu,Daisuke Morokuma,Kazuma Hirata,Mami Yamashita,Noriko Karasaki,Tuneyuki Tatsuke,Hiroaki Mon,Kazuhiro Iiyama,Noriho Kamiya,Yutaka Banno,Takahiro Kusakabe,이재민 한국응용곤충학회 2016 Journal of Asia-Pacific Entomology Vol.19 No.2
Interleukin 2 (IL-2) is a pharmacologically vital cytokine secreted mainly by activated CD4+ T lymphocyte. Recombinant human IL-2 (rhIL-2) protein has already been globally applied as an immune-therapeutic reagent for various diseases. Therefore, there is great interest in developing an active form of rhIL-2 in very large amounts and with excellent purity for clinical use. In this study, we successfully mass-expressed and purified N- or C-terminal tandem tag-fused rhIL-2 in a baculovirus expression vector system (BEVS) using silkworm larvae as factories. We confirmed that the intrinsic instability of hIL-2 causes the loss and low recovery of N-tagged rhIL-2 and that C-tagged rhIL-2 ismore suitable for mass production. Furthermore, the activity of purified rhIL-2s was further validated by a cell proliferation assay of a human natural killer cell line, and both rhIL-2 proteins produced in the silkworm-BEVS exhibited comparable activity to that of the commercial E.coli-derived rhIL-2. Taken together, our results and strategies could contribute greatly to the mass production of active rhIL-2.