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벤질아민을 기질로 사용한 뇌 Monoamine Oxidase 의 기초 성질
박희섭,최명언 ( Heeseob Park,Myung Un Choi ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.3
Monoamine oxidase (MAO) of rat brain was assayed by spectrophotometric method using benzylamine as substrate. Basic assay condition was optimized and the specific activity of prepared mitochondrial fraction was 2 nmoles/㎎ protein/min. under the standared condition. In order to correlate the MAO activity with the physico-chemical state of mitochondria, the enzyme activity was assayed in the presence of various chemicals known to affect the metabolic state of mitochondria. Among the tested, the proton and Ca^(+2) ion exibited interesting results. When pH was altered from 7.2 to 9.0, the activity of the brain MAO increased more than twofold and the calculated Km value at the alkaline pH was about 5 times smaller than that of neutral pH. Thus the Vmax/Km profile indicates that the neutral molecule appears to be the active substrate. Ca^(+2) ion showed moderate activation of the brain MAO activity at pH 7.2×9.0 in Tris-HCl buffer. When the mitochondrial MAO was solubilized with Triton X-100, the Ca^(+2) ion effect disappeared.
Hidden Markov Model에 기반한 기업의 국면변화과정 분류 -KOSPI200을 대상으로-
박희섭,이계민 한국자료분석학회 2004 Journal of the Korean Data Analysis Society Vol.6 No.6
We present a way to classify the corporations registered at KOSPI200 into several groups having similar stock price changing patterns. We first estimate each individual corporation's regime-change-process which reflects changes in the corporation's daily prices through a hidden markov model. We then calculate the correlation coefficient matrix of the estimated regime-change-processes of the corporations. Finally, we classify the corporations into several groups applying the cluster analysis. Based on these three procedures, we can obtain a number of groups having similar stock price changing patterns. This result is expected to be a useful tool for constructing efficient portfolios. 본 논문에서는 KOSPI200에 등록된 기업들을 유사한 주식가격의 변화패턴을 가지는 몇 개의 그룹으로 분류하였다. 이를 위해 다음 작업들을 수행하였다. 첫째, 일일종가의 변화에 내재된 개별기업의 국면변화과정을 Hidden Markov Model를 통해 추정하였다. 둘째, 추정된 국면변화과정을 이용해 기업간 상관계수를 구하였다. 끝으로, (1-상관계수)를 거리개념으로 사용하여 기업을 군집분석하였다. 동일 그룹으로 분류된 기업은 동일한 주가의 변화패턴을 가지는 것으로 볼 수 있다. 따라서, 몇 개의 그룹으로 분류된 군집분석의 결과는 포트폴리오를 구성할 때 도움을 줄 것으로 기대된다.
단일항체 칼럼과 고압 액체크로마토그래피에 의한 유전자 조작 사람 알파 인터페론의 분리 및 정제
박희섭,정미영,오명석,고중환,김현수,현형환 ( H . S . Park,M . Y . Jung,M . S . Oh,J . H . Koh,H . S . Kim,H . H . Hyun ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.4
Immunoadsorbent chromatography technique was applied for the efficient purification of Interferon (rIFN-α) from recombinant E. coli. Monoclonal antibody to rIFN-α was purified using protein A-Sepharose CL-4B chromatography from ascites fluid of BALB/c mice which were innoculated with monoclonal hybridoma cell. The purified antibody was coupled to Affigel-10, and used as an immunoadsorbent for IFN. The recombinant E. coli cells were sedimented and cell-opening was done using 6 M guanidine-HCl. It was loaded to the above immunoadsorbent column and then the bound IFN was eluted from the column with 0.2 M acetic acid. As a result of purification, the specific activity of the purified IFN was 2 × 10^8 IU/㎎ protein and the purification fold was 4100. The amino-terminal sequence of purified IFN was exactly identical to that of natural human leukocyte IFN upto 30 amino acid residues except the lst and 29th unidentified amino acid residues. The molecular weight of the purified IFN was estimated to be 18,600 by SDS-PAGE. Since IFN purified by monoclonal antibody column contains IFN dimer up to 15% further purification was done by HPLC gel filtration. The purity of finally-purified IFN monomer was estimated to be more than 99.9% by SDS-PAGE under non-reducing condition. Finally-purified IFN monomer has several pI points (6.12, 6.06, 5.85, 5.58, and 5.30).
박희섭,정미영,오명석,고중환,김현수,현형환,Park, H.S.,Jung, M.Y.,Oh, M.S.,Koh, J.H.,Kim, H.S.,Hyun, H.H. 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.4
유전자 조작된 대장균이 생산하는 알파 인터페론을 단일 항체 칼럼을 사용하여 효과적으로 정제하였다. rIFN-$\alpha$에 대한 항체를 생산하는 단일클론 융합세 포를 쥐(BALB/c)의 복강에 접종하여 얻은 복강액으로부터 Protein A column을 사용하여 항체를 정제하였다. 이 정제된 항체를 Affigel-10에 결합시켜 단일항체 칼럼을 만든 후, 유전자 조각 장균을 6M 구아니딘 (guanidine-HCl)으로 처리 하여 얻은 인터페론 포함 상등액을 통과시켜 인터페론을 정제하였다. 정제된 인터페론 $2{\times}10^8\;IU/mg$ protein의 specific activity를 가졌으며 분자량은 SDS-PAGE에서 18,600이었고 30개까지 이이노산 서열을 분석한 결과 천연의 human leukocyte IFN-$\alpha$의 것과 동일하였다. 비환원 조건에서 SDS-PAGE 한 결과 약 15%의 인터페론 이중체 (Interferon dimer)를 포함 하고 있었다. 이를 제거하기 위해 생리식염수 용액으로 사용하여 HPLC 젤여과를 행하였다. 최종 정제된 인터페론을 비환원 조건에서 SDS-PAGE 한 결과 인터페론 단일체의 순도는 99.9% 이상인 것으로 판명되었으며, 최종 정제된 인터페론은 약 5개의 등전 전위점을 갖고 있다 (pI = 6.12, 6.06, 5.85, 5.58, 5.30). Immunoadsorbent chromatography technique was applied for the efficient purification of Interferon (rIFN-$\alpha$) from recombinant E. coli. Monoclonal antibody to rIFN-$\alpha$ was purified using protein A-Sepharose CL-4B chromatography from ascites fluid of BALB/c mice which were innoculated with monoclonal hybridoma cell. The purified antibody was coupled to Affigel-10, and used as an immunoadsorbent for IFN. The recombinant E. coli cells were sedimented and cell-opening was done using 6 M guanidine-HCl. It was loaded to the above immunoadsorhent column and then the bound IFN was eluted from the column with 0.2 M acetic acid. As a result of purification, the specific activity of the purified IFN was $2{\times}10^8\;IU/mg$ protein and the purification fold was 4100. The amino-terminal sequence of purified IFN was exactly identical to that of natural human leukocyte IFN upto 30 amino acid residues except the 1st and 29th unidentified amino acid residues. The molecular weight of the purified IFN was estimated to be 18,600 by SDS-PAGE. Since IFN purified by monoclonal antibody column contains IFN dimer up to 15%, further purification was done by HPLC gel filtration. The purity of finally-purified IFN monomer was estimated to be more than 99.9% by SDS-PAGE under non-reducing condition. Finally-purified IFN monomer has several pI points (6.12, 6.06, 5.85, 5.58, and 5.30).
Basic Properties of Brain Monoamine Oxidase Using Benzylamine as Substrate
박희섭,최명언,Park, Hee-Seob,Choi, Myung-Un 생화학분자생물학회 1983 한국생화학회지 Vol.16 No.3
쥐 뇌의 monoamin oxidase(MAO)를 benzylamine을 기질로 하여 분광학적 방법으로 측정했다. 먼저 기본적인 정량조건을 수렵했으며 이 조건하에서 분리된 mitochondria 에서의 MAO 활동도는 2nmoles/분/mg 단백질 정도였다. MAO 의 활동도와 mitochondria의 물리-화학적 상태와의 연관성을 알아 보기 위해 여러 종류의 화학물질들의 영향을 관찰했다. 검토된 중에서 수소와 $Ca^{+2}$ 이온의 영향이 흥미롭게 나타났다. pH가 7.2에서 9.0으로 변하면 MAO의 활동도는 두 갑절이상 증가하며 알카리성일때 계산된 Km 값은 산성일때의 것과 비교 다섯 갑절 정도 적게 나타났다. 따라서 Vmax/Km은 중성분자가 실제로 활성이 있는 기질임을 암시해 주고 있다. pH 7.2와 9.0사이에서 $Ca^{+2}$ 이온은 뇌 MAO의 활동도를 어느 정도 증가시켰으며, 이 효소가 Triton X-100로 용해되었을 경우 이 $Ca^{+2}$ 이온 효과는 없어졌다. Monoamine oxidase (MAO) of rat brain was assayed by spectrophotometric method using benzylamine as substrate. Basic assay condition was optimized and the specific activity of prepared mitochondrial fraction was 2 nmoles/mg protein/min. under the standared condition. In order to correlate the MAO activity with the physico-chemical state of mitochondria, the enzyme activity was assayed in the presence of various chemicals known to affect the metabolic state of mitochondria. Among the tested, the proton and $Ca^{+2}$ ion exibited interesting results. When pH was altered from 7.2 to 9.0, the activity of the brain MAO increased more than twofold and the calculated Km value at the alkaline pH was about 5 times smaller than that of neutral pH. Thus the Vmax/Km profile indicates that the neutral molecule appears to be the active substrate. $Ca^{+2}$ ion showed moderate activation of the brain MAO activity at pH 7.2~9.0 in Tris-HCl buffer. When the mitochondrial MAO was solubilized with Triton X-100, the $Ca^{+2}$ ion effect disappeared.