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Application and Genetic Engineering of Insecticidal Gene
Lee,Hyung-Hoan 中央大學校 遺傳工學硏究所 1989 遺傳工學硏究論集 Vol.2 No.1
A recombinant plasmid was constructed by ligating Eco R1 2.0kb DNA fragment containing the mosquitocidal crystalline protein(MCP)gene from B.sphaericus chromosome into the Eco R1 site of the vector pUC-8 and transformed into Escherichia. coli. Four transformants showed lethality to Culex pipiensis larvae. The clones were named pSL-2, -5, -6 and -8. The clone pSL-2 contained a 2kb DNA fragment from the B.sphaericus chromosome,in which the MCP gene resided. The LC50 of the MCP produced by the pSL-2 clone was about 50 times (500ng/ml) lower than that (9ng/ml) produced by B.sphaericus The unsolubilized mosquitocidal crystal proteins from the B.sphaericus had formed 43, 58, 64, 100, 113 and 130kd bands in the SDS-polyacrylamide gel, but the NAOH-solublized proteins at PH 12 formed 2 protein bands of 43-and 64kb in the gel because the larger protein (precusor) bands were cleaved. The products of the pSL-2-1 clone was purified by Sephadex G-200 and only the fractions having lethal activity to the 3rd instar larvae of mosquito Culex pipiens were analyzed by the gel. The only single protein band of 42kd toxic to the larvae was formed. the major toxic protein being produced from the B.sphaericus 1593 and the pSL-2-1 clone was found to be the 42kd.
Replication of Autographa californica Nuclear Polyhedrosis Virus ts - B1074
Lee, Hyung Hoan,Oh, Chang Keun,Lee, Keun Kwang 한국유전학회 1989 Genes & Genomics Vol.11 No.4
Replication sequences of Autographa californica Nuclear Polyhedrosis Virus ts-B1074 at 25℃ and 32.5℃ were comparatively visualized at time intervals from 0 to 48 h postinfection. The nucleocapsids adsorbed onto the host cell surface within 30 min, penetrated into the cytoplasm within 60 min and passed through the cytoplasm to the nuclear membrane within 2 h postinfection. Eclipse period was occurred from 4 to 10 h postinfection. At 10 h virogenic stroma were formed. At 13 h postinfection, progeny nucleocapsides were appeared and budded. At 18 h prepolyhedral proteins were appeared. At 30 h the normal polyhedra were matured and occluded by enveloped nucleocapsids, but the polyhedra of the ts mutant were abnormal at 32.5℃. Therefore the enveloped nucleocapsids were not occluded onto them.
Induction and Characterization of Lysine Decarboxylase from Serratia marcescens
Lee,Hyung-Hoan 建國大學校附設 應用科學硏究所 1979 理學論集 Vol.5 No.-
Serratia marcescens 와 Salmonella newport 균주는 Salt배양액에서 배양되었다. 배양액 조성의 변경에 의하여, 즉 l-lysineㆍHCl과 Casein 분해물의 첨가로 S.marcescens 와 S. newport의 l-lysine decarboxylase의 유도는 상승적으로 작용하였고, 그리고 더우기 그 induction medium서 만들어진 단백질의 양과 박테리아의 수는 control medium 보다 거의 세배가 더 크게 나타났다. 효소 l-lysine decarboxylase 는 Serratia marcescens를 분쇄하여 추출하였고, 이 효소와 l-lysineㆍHCl과의 반응에서 Michaelis constant는 거의 0.003M, 효소활동을 위한 최적온도는 약 55℃, 최적 pH는 6.5인 것으로 나타났다.