http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
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.
신성문,이종협,최문기,Sin, Seong-Mun,Lee, Jong-Hyeop,Choe, Mun-Gi 한국전자통신연구원 1992 전자통신 Vol.14 No.4
It is indispensable to control the service traffic for maximizing the advantages of ATM. This paper introduces the scheme of the an ATM traffic control and investigates the UPC(Usage Parameter Control) algorithms of the ATM-traffic. We have extracted the considerations on UPC algorithms and described the definition of the performance. We also have searched the way to choose the most appropriate UPC method considering the UPC's environments. As a result, we proposed the reliable UPC method that is applicable to B-ISDN, based on the comparison of the performance and the implementation of each.
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.