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노시갑,선희숙,伴野 豊 한국잠사학회 1998 한국잠사곤충학회지 Vol.40 No.1
Studies were carried out to investigate phenotypic expression, mortality and biochemical analysis of haemolymph proteins of nm-d, nm-f, nm-i, nwr-k and nmn non-molting mutants of the silkworm, Bombyx mori. The non-molting mutants characters were expressed in the homozygote of each mutant genes. All strains of non-molting mutants were similar with each other in physiological characteristics, but the expression varied with each strains. The larvae of nm-d, nm-i and nwfn died between day 5 and day 9 after hatching without the first molt. The nm-f and nm-k mutants died between day 5 and day 16 with a slight increase of body weight and, more than 90% of the mutants larvae died before the first molt and a few of them survived to the 2nd and the 3rd instar and died. The haemolymph protein components of nm-d,nm-i and nmn were rapidly reduced , and on the other hand those of nm-f and nm-k consistently until they died. And there were no distinguishable difference in haemolymph components of non-molting mutants, as compared to those of normals.
Atsushi Masuda,Jian Xu,TakumiMitsudome,Daisuke Morokuma,Hiroaki Mon,Yutaka Banno,Takahiro Kusakabe,이재만 한국응용곤충학회 2015 Journal of Asia-Pacific Entomology Vol.18 No.2
Endo-β-N-acetylglucosaminidase H (Endo H) catalyzes cleavage between the GlcNAc residues of the chitobiose core of N-linked glycans, leaving one GlcNAc residues attached to asparagine. Endo H cleaves high mannose and hybrid, but not complex, N-linked oligosaccharides on glycoproteins. Because of its unique specificity, Endo H is widely used for the structural and functional analyses of glycoproteins. In our previous study, the recombinant Endo H was produced as a secreted protein using silkworm–baculovirus expression system, but the yield was low (30 μg Endo H/10 ml larval hemolymph) compared to that of Escherichia coli. In this study, we purified active recombinant Endo H as an intracellular protein from fat body of silkworm infected with the recombinant baculovirus expressing Endo H without the exogenous signal peptide. Remarkably, the yield (9.3mgfrom20 silkwormlarvae)was about 310-fold higher than that secreted into larval hemolymph as reported previously. In addition,we screened the silkwormstrains maintained in Kyushu University and identified n17 as a high-level expression strain for Endo H.
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.
Jee-Young Pyo,Jeong Sun Park,Min Jee Kim,Heon Cheon Jeong,Sung-Soo Kim,Yutaka Banno,Seung Hyun Lee,Min Woo Park,Iksoo Kim 한국응용곤충학회 2023 한국응용곤충학회 학술대회논문집 Vol.2023 No.10
Bombyx mandarina (Lepidoptera: Bombycidae), the presumed ancestor of B. mori, has long been a subject of study to illustrate the geographic relationships in connection with origin of B. mori. We report 97 mitochondrial genome (mitogenome) sequences of B. mandarina collected from Korea and Japan. Phylogenetic and population genetic analyses showed that all individuals of B. mandarina collected in Korean localities formed a strong group together with all individuals originated from northern China (mainly north of the Qinling-Huaihe line) and some of southern China. This group was placed as the sister group to B. mori strians suggesting that this group had been served as an immediate progenitor for B. mori.
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.