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Purification of Human Interferon-${\beta}$ from Recombinant E. coli
이진규,이석재,최문기,정광회,신광순,백승복,Lee, Jin-Kyu,Lee, Seok-Jae,Choe, Moon-Kee,Chung, Kwang-Hoe,Shin, Kwang-Soon,Paik, Sung-Bok 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.2
유전자 재조합 인간 Interferon-${\beta}$를 초음파 처리, 8 M Guanidine-HCl 추출, inclusion body의 용해, 희석, Blue Sepharose CL-6B column chromatography, HPLC gel filtration 방법 등을 이용하여 대장균으로부터 정제하였다. 정제된 IFN-${\beta}$의 specific activity는 $3.1{\times}10^8$ IU/mg이었고 정제도는 1,902이었다. 정제된 IFN-${\beta}$는 환원된 상태와 환원되지 않은 상태에서 SDS polyacrylamide gel electrophoresis 한 결과 모두 단일 띠로 나타났으며 분자량은 18,000 dalton이었다. N-말단 아미노산을 조사한 결과 재조합 인간 IFN-${\beta}$는 천연형 인간IFN-${\beta}$와 같이 N-말단이 methionine임이 밝혀졌다. 전자 현미경을 이용하여 inclusion body 형성을 조사한 결과 IFN-${\beta}$ 유전자를 가지고 있는 대장균에서는 inclusion body의 형성을 확인할 수 있었으나 숙주(wild type)에서는 확인되지 않았다. 최종적으로 정제된 IFN-${\beta}$의 정제도는 HPLC gel filtration 한 결과 99% 이상으로 나타났다. Recombinant human interferon-${\beta}$ was purified to homogeneity from E. coli by methods of sonication, extraction with 8 M Guanidine HCl, solubilization of inclusion body, dilution, Blue Sepharose CL-6B column chromatography and HPLC gel filtration. Specific activity of purified IFN-${\beta}$ was $3.1{\times}10^8$ IU/mg protein and the purification was 1,902 fold. The purified IFN-${\beta}$ was a single band on SDS polyacrylamide gel electrophoresis under reducing condition and non-reducing condition and its molecular weight was estimated to 18,000 dalton. The results of N-terminal analysis showed that recombinant human IFN-${\beta}$ has N-terminal methionine same as natural human IFN-${\beta}$. The inclusion bodies were observed in the E. coli cells harboring IFN-${\beta}$ gene but not observed in the host cells (MM 294). The purity of finally purified IFN-${\beta}$ was more than 99% by HPLC gel filtration.
유전자 재조합 대장균으로부터 인간 Interferon - β
이진규,이석재,최문기,정광희,신광순,백승복 ( Jin Kyu Lee,Jae Lee,Moon Kee Choe,Kwang Hoe Chung,Kwang Soon Shin,Sung Bok Paik ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.2
Glutathione S-transferase ρ (EC 2.5.1.18) has been purified to homogeneity from human erythrocytes. A combination of gel filtration, ion exchange and hydroxylapatite chromatographic procedure yields the specific activity of 20.8 units/㎎. The purified enzyme gives a single band corresponding to 24,000 M.W. on a sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme molecule is characterized to be an acidic protein (pI 4.6) having a dimeric structure with 48,000 M.W. composed of identical size of polypeptide chains. Apparent K_m and V_(max) were determined to be 1.1 mM and 1.0 mmol/1/min for 1-chloro-2,4-dinitro benzene respectively while 0.3 mM and 0.55 mmol/l/min for glutathione. Results obtained from chemical modification studies suggest that essential amino group(s) critically connected to the catalytic function of glutathione S-transferaseρ.
인플루엔자 바이러스의 Neuraminidase 抗原分析
白承福 건국대학교 1976 論文集 Vol.3 No.1
1.The influenza virus strains isolated in Korea in 1971 and 1972 were experimented for their antigenic analysis by Neuraminidase-Inhibition test. 2.A/NWS(H0N2), a variant strain of A/Pa/8/34(H0N1) was used as a N2 reference virus strain and A/0318(H0N2), a recombinant strain of AJNWS(H0N2) and A/Aichi/2/68 (H3N2) was used as a Na reference virus strain. Strain specific antisera were prepared in adult chicken in which H-I titer of 1 : 2048 or more were used as for reference antisera. 3.The obtained results of the tests are summarized as follows : all the methods used in the tests were followed by standard methods of Center far Disease Control in USA. a) Neuraminidase assay tests ; The virus dilution numbers corresponding to O.D. 0.850 of each strains were 1 : 8.5 in NWS(H0N1),1 :10 in 0318(H0N2), 1 :14 in A/Korea/71 and 1 : 7.4 in A/Korea/72. b) Neuraminidase-Inhibition tests ; The titers of 70% neuraminidase-inhibition activity of each antiserum against corresponding antigens were indicated in the following table. ◁표 삽입▷ (원문을 참조하세요) 4.As shown in the above table, it was identified that A/Korea/71 and A/Korea/72, isolated strains were belonged to N2 subtype of Influenza A.
Production of Anti-Hepatitis B Surface Antigen Monoclonal Antibody in Serum-Free Medium
Chun, Bok Hwan,Jo, Eui Cheol,Kim, Dong Il,Paik, Sung Bok 한국산업미생물학회 1990 한국미생물·생명공학회지 Vol.18 No.2
간염 바이러스 표면 항원에 대한 단일클론 항체를 생산하는 하이브리도마 세포 2c3.1의 대량배양을 위하여 무혈청 배지를 조성하였다. 2c3.1 세포를 RPM1 1640 배지와 Ham's F12 배지의 여러 부피비에 배양함으로써 세포성장이 가장 좋은 비의 배지를 기본 영양배지로 선택하였다. 세포 성장을 증가시키기 위하여 무혈청 배지 첨가물들을 여러 농도로 변화시켜 기본영양배지에 첨가함으로써 각 첨가물들의 농도를 결정하였다. 무혈정 배지 첨가물은 0.45% 인혈청 알부민, 10㎍/㎖ insulin, 10㎍/㎖ transferrin 등을 사용하고, 0.17㎍/㎖ fat emulsion(Intralipos^R:0.125㎍/㎖ soybean oil, 0.015㎍/㎖ ovolecithin, 0.03㎍/㎖ glycerin), 0.01㎍/㎖ 비타민 E와 0.02㎍/㎖ 비타민 E 아세테이트, 그리고 10uM monoethanolamine 등의 적정 농도를 2c3.1 세포의 무혈청 배양에 사용하였다. 이 무혈정 배지에서 대수 증가적으로 증식하는 하이브리도마 세포는 10% 우태아혈청을 사용한 배지에서 보다 비증식속도와 최대 세포농도에서 다소 낮으나, 단일클론항체는 혈청 사용 배지의 43㎍/㎖보다 다소 높은 50㎍/㎖가 생성됨으로써 이 하이브리도마로부터 단일클론항체를 생산하기 위하여 조성된 무혈정 배지가 10% 우태아혈청 배지를 대신할 수 있음을 보였다. For the large-scale cultivation of murine hybridoma 2c3.1 cells secreting anti-Hepatitis B surface antigen(anti-HBsAg)monoclonal antibody(MAb), we have constructed a serum-free medium. The serum-free medium was supplemented with human serum albumain, insulin, transferrin, fat emulsion(Intralipos^R:soybean oil, ovolecithin, glycerin), vitamin E, vitamin E acetate, and monoethanolamine in a mixture of RPMI 1640 and Ham's F12 medium. The cells in serum-free medium propagated logarithmically without lag period, and the maximum concentration of anti-HBsAg monoclonal antibodies secreted by 2c3.1 cells was higher than that in 10% fetal bovine serum(FBS) medium. The serum-free medium was enough to substitute 10% FBS medium in respect of MAb production.
한국에서 분리된 렙토스피라균의 생물학적 특성에 대한 연구(1985)
이용우,이명숙,백승복,박미연,박경석,오희복,김호훈,성원근 대한미생물학회 1986 大韓微生物學會誌 Vol.21 No.3
A microbiological study for the isolation and characterization of Leptospira interrogans was performed in an attempt to define the characteristics of Leptospirosis in Korea. The results are summerised as follows. Thirty-five cultures were isolated from 11 patients with leptospirosis and 24 wild rodents captured in Paju area. The isolation rate of Leptospira from wild rodents reached 23.1%. All 35 cultures were identified as Leptospira interrogans by their characteristic morphology and motility in dark field microscopy, pathogenecity in Guinea pig and sensitivity to S-Azaguanine. Cultures formed diffuse subsurface colonies with hazy margin and were catalase, peroxidase and ox- dase positive. The fifty percent lethal dose of isolate HM 4 in Guinea pig was 8.9X10_4 org. Mouse passage method was sucecssfully applied in maintenance of fresh isolates without any loss of their original virulency.