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조은숙,진병래,손흥대,강석우,윤은영,김근영,제연호,강석권 한국생명과학회 1998 한국생명과학회 학술발표회 Vol.20 No.-
To construct transformed BmN cells, Autographa californica nuclear polyhedrosis virus (AcNPV) IE1 gene, an immediate early viral gene was firstly used in this study. AcNPV IE1 gene, which shares on 95.3% nucleotide sequence homology with Bombyx mori nuclear polyhedrosis virus (BmNPV) IE1, was isolated and cloned into pUC18. Neomycin gene from pNeo was inserted under the control of the IE1 promoter to yield pAcIE1-neo. The plasmid pAcIE1-neo was transfected into BmN cells and neomycin-resistant cells were selected in TC100 medium containing 10% FBS and 1㎎/㎖ G418 for two weeks. Individiual colonies were picked and each was amplified for further characterization. The genomic DNA from neomycin-resistant cells was isolated and characterized by PCR using AcNPV IE1 gene-specific primers and by Southern blot analysis using neo gene probe. We concluded that AcNPV IE1 gene was functional in B. mori-derived BmN cells as well as Spodopterafrugiperda-derived Sf9 cells to produce stably-transformed insect cells.
조은숙,박해진,진병래,손흥대,강석우,윤은영,김근영,제연호,강석권 한국생명과학회 1998 한국생명과학회 학술발표회 Vol.20 No.-
To analysis a promoter strength of Autographa californica nuclear polyhedrosis virus (AcNPV) IE1 gene, an immediate early viral gene, β-galactosidase gene as a reporter gene was introduced under the control of the IE1 promoter. The restriction fragment containing IE1 promoter and β -galactosidase gene from pAcIE1-gal was inserted into pBacPAK8 to yield transfer vector pAcNPV-IE1-gal. The pAcNPVIE1-gal was cotransfected with AcNPV genomic DNA BacPAK6 into Sf9 cells to produce recombinant baculovirus AcNPV-IE1-gal. In addition, recombinant baculovirus AcNPV-gal, which express β-galactosidase under the control of the polyhedrin promoter, was constructed to compare with AcNPV-IE1-gal. The recombinant viruses were respectively infected into Sf9 cells and characterized by the virus titer and expression of β-galactosidase in Sf9 cells. The promoter strength between IE1 and polyhedrin promoters was determined by the amount of the secreted β-galactosidase into medium.. The titer of AcNPV-IE1-gal determined by plaque assays in Sf9 cells was similar to that of AcNPV-gal. However, expression level of β -galactosidase by AcNPV-IE1-gal was significantly lower than that expressed by AcNPV-gal. In conclusion, promoter strength of IE1 was approximately 25-fold lower than that of polyhedrin promoter.
Shin, Byung Sik,Lee, Choong Un,Koh, Jin Bog,Shon, Hung Dae 고려대학교 한국곤충연구소 1995 昆蟲硏究誌 Vol.21 No.1
The cold-hardiness mechanisms-the changes of carbohydrates, lipid, amino acids concentrations -of in the greater wax moth, Galleria mellonella were examined during 2 weeks acclimation at tow temperatures (15˚C, 5˚C, and 0˚C). Glycogen levels were shown to be remarkable decreases at 0˚C (9.260 ㎍/50 ㎕) as compared to 15˚C (38.106 ㎍/50 ㎕) and 5˚C (52.189 ㎍/50 ㎕). The highest levels of glycerol (0.414 ㎍/50 ㎕) and glucose (0.448 ㎍/50 ㎕) were measured at 0˚C, but the glycogen content was extremely decrease at same temperature. On the other hand, trehalose was present in large devrease at 5˚C in comparision with 15˚C, began to increase in small concentration at 0˚C. Identified lipid components were triglyceride, monoglyceride, fatty acid, sterol, and phospholipid. Triglyceride concentration was 55% of its maximum (35.77 ㎍/30 ㎕, 5˚C) in the larvae at 0˚C (19.05 ㎍/30 ㎕), other lipid components generally decreased in amount at 5˚C. The levels of 15, 16, and 13 free amino acids were detected at 15˚C, 5˚C and 0˚C. High value of identified amino acids were glutamic acids, glycine, threonine, alanine, proline, tryptophan and lysine. The highest level of proline was separated at all temperature conditions, its relative rates in amino acids composition were 18.20% (15˚C), 14.93% (5˚C), and 25.53% (0˚C). In this results, high level of glycerol and glucose concentration with acclimation to low temperatures were thought to be related to the freezing tolerance, in addition amino acids, such as proline, glycine and lysine were regarded as assistant roles.
( Gui Zhong Zheng ),( Bo Yeon Kim ),( Hyung Joo Yoon ),( Ya Dong Wei ),( Guo Xi Jie ),( Byung Rae Jin ),( Hung Dae Shon ) 한국잠사학회 2007 International Journal of Industrial Entomology Vol.14 No.1
In a previous study, three larval cuticle protein genes were cloned from the mulberry longicorn beetle, Apriona germari (Comp. Biochem. Physiol. B 136,803-811, 2003). In the present study, the genomic structures of these three larval cuticle protein genes (AgLCP9.2, AgLCP12.6 and AgLCP12.3) were elucidated. All three cuticle protein genes consist of one intron and two exons. Southern blot analysis of genomic DNA suggested that three cuticle protein genes are a single copy gene. In addition, a novel larval cuticle protein gene, AgLCP10.6, was cloned from A. germari in this study. The AgLCP10.6 cDNA contains an ORF of 300 nucleotides that are capable of encoding a 100-amino acid polypeptide with a predicted molecular mass of 10.6 kDa. The amino acid sequence deduced from the AgLCP10.6 cDNA contained a type-specific consensus sequence identifiable in other insect cuticle proteins and is most homologous to Drosophila melanogaster cuticle protein ACP65A (51 % protein sequence identity). Northern blot analysis revealed that AgLCP10.6 showed epidermis-specific expression.
Purification and Characterization of Vitellin from the Red Flour Beetle, Tribolium castaneum Herbst
Kim, Seong-Ryul,Choo, Young-Moo,Lee, Seong-Jin,Jin, Byung-Rae,Kim, Jeong-Ho,Heo, In-Bum,Shon, Hung-Dae Korean Society of Sericultural Science 2001 International Journal of Industrial Entomology Vol.2 No.1
The vitellin of the red flour beetled Tribolium castaneum Herbst was purified and characterized. The vitellin of T. castaneum was purified by the FPLC techniques, anion exchange chromatography and gel permeation chromatography. In native-polyacrylamide gel electrophoresis, vitellin of T. castaneum was detected as a single band. This native vitellin has molecular weight of 440 kDa. The vitellin of T. castaneum is composed of three polypeptides, designated Vnl (178 kDa), Vn2 (168 kDa) and Vn3 (52 kDa) in SDS-polyacrylamide gel electrophoresis. Three subunits of vitellin were presented in the female adult hemolymph and egg extracts, but not observed in the male. These three polypeptides gradually decreased during embryogenesis. Polyclonal antiserum raised against purified vitellin reacted with the three polypeptides, Vnl, Vn2 and Vn3. Antisera raised against Vn1 and Vn2 cross-reacted with the two large subunits, Vnl and Vn2, respectively. Another subunits Vn3, however, was not cross-reacted with these two antisera. Also, antiserum raised against Vn3 did not cross-react with the Vn1 and Vn2.
Zheng Gui Zhong,Kim Bo-Yeon,Yoon Hyung-Joo,Wei Ya Dong,Xijie Guo,Jin Byung-Rae,Shon Hung-Dae Korean Society of Sericultural Science 2007 International Journal of Industrial Entomology Vol.14 No.1
In a previous study, three larval cuticle protein genes were cloned from the mulberry longicorn beetle, Apriona germari (Comp. Biochem. Physiol. B 136, 803-811, 2003). In the present study, the genomic structures of these three larval cuticle protein genes (AgLCP9.2, AgLCP12.6 and AgLCP12.3) were elucidated. All three cuticle protein genes consist of one intron and two exons. Southern blot analysis of genomic DNA suggested that three cuticle protein genes are a single copy gene. In addition, a novel larval cuticle protein gene, AgLCP10.6, was cloned from A. germari in this study. The AgLCP10.6 cDNA contains an ORF of 300 nucleotides that are capable of encoding a 100-amino acid polypeptide with a predicted molecular mass of 10.6 kDa. The amino acid sequence deduced from the AgLCP10.6 cDNA contained a type-specific consensus sequence identifiable in other insect cuticle proteins and is most homologous to Drosophila melanogaster cuticle protein ACP65A (51 % protein sequence identity). Northern blot analysis revealed that AgLCP10.6 showed epidermis-specific expression.