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Thermus caldophilus GK24 DNA Polymerase를 이용한 Polymerase Chain Reaction의 최적조건
권석태 성균관대학교 생명과학자원연구소 1994 生命資源科學硏究 Vol.1 No.1
A thermostable DNA polymerase was used in an in vitro amplification procedure, the polymerase chain reaction(PCR). Thermus caldophilus GK24(Tca) DNA polymerase greatly simplifies the procedure and, by enabling the amplificatioin reaction to be performed at higher temperature, significantly improves the specificity, yield and sensitivity. The optimal conditions for PCR were investigated in terms of pH range, MgCl_2, KCl and DTT concentration using the purified Tca DNA polymerase. The optimal pH for DNA amplification was found to be between 8.6, and 9.2 in 50mM Tris-HCl buffer. The optimal concentrations of MgCl_2 and KCl for PCR were 1-1.5mM and 10-50mM, respectively. The concentration of DTT above 0.5mM was sufficient to amplify template DNA by PCR. These conditions can be used to amplify a wide range of target sequences with excellent specificity.
대장균에서 Thermus caldophilus GK24의 DNA Polymerase유전자의 고발현
권석태,김현규,김중수,이대실 성균관대학교 생명과학자원연구소 1997 生命資源科學硏究 Vol.4 No.2
Thermus caldophilus GK24 (Tca) DNA polymerase is highly useful enzyme for amplifying DNA fragments by polymerase chain reaction (PCR). A plasmid, pTCA, is expression vector for Tca DNA polymerase gene in Escherichia coli under the control of tac promoter and its expression level is low. For the high expression, the DNA sequence coding for NH_2-amino acid sequence of Tca DNA polymerase was changed by PCR, and then an expression vector pTCAM was constructed. The activity of Tca DNA polymerase in E. coli harboring for pTCAM has enhanced nearly 6-fold/ml than that for E. coli harboring pTCA.
Thermus aquaticus YT - 1 의 내열성 프로테아제 aqualysin Ⅰ 의 구조와 특징
권석태 한국농화학회 1988 Applied Biological Chemistry (Appl Biol Chem) Vol.31 No.3
Aqualysin I is an alkaline serine protease which is secretet into the culture medium by Thermos aquaticus YT-1, an extreme thermophile. Aqualysin I was purified, and its partial amino acid sequence was determined. The gene encoding aqualysin I was cloned into E. coli using synthetic oligodeoxyribonucleotides as hybridization probes. The nucleotide sequence of the cloned DNA was determined. The primary structure of aqualysin I, deduced from the nucleotide sequence, agreed with the determid amino acid sequences, including the NH₂- and COOH terminal sequence of the tryptides derived from aqualysin I. Aqualysin I comprised 281 amino acid residues and its molecular mass was determined to 1)e 28350. On alignment of the whole amino acid sequence, aqualysin I showed high sequence homology with the subtilisin type serine protease, and 43% identity with proteinase K, 37-30% with subtilisins and 34% with thermitase. Extremely high sequence identity was observed in the regions containing the active-site residues, corresponding to Asp32, His64 and Ser221 of subtilisin BPN'. Aqualysin I contains two disulfide bonds, Cys67-Cys99 and Cys163-Cysl94, and these disulfide bonds seem to contribute to the heat stability of the enzyme. The determined positions of the twe disulfide bonds of aqualysin I agreed with those predicted previously on the basis of computer graphics of the crystallographic data for subtilisin BPN'. Therefore, these findings sugests that the three-dimensional structure of aqualysin I is similar to that of subtilisin BPN' Aqualysin I is produced as a lage precursor, which contains NH₂- and COOH- terminal portions besides the mature protease sequence.
Thermus flavus AT-62 균주의 내열성 DNA Ligase 유전자의 Cloning 및 발현
권석태 성균관대학교 생명과학자원연구소 1994 生命資源科學硏究 Vol.1 No.1
The DNA fragment encoding DNA ligase from Thermus flovus AT-62 was cloned into Escherichia coli using polymerase chain reaction(PCR) method. Under tac promoter control, Thermus flavus AT-62(Tfl) DNA ligase was expressed in E colt. Tfl DNA ligase in E. coli was purified by simple methods like heat treating, DEAESephacel and Cellulose phosphate column chromatography. The purified enzyme had a molecular mass of about 77kDa, estimated by sodium dodecyl sulfate-polyacrylamide-gel electrophoresis. The purified Tfl DNA ligase was capable of catalyzing blunt-end ligation at 65℃.
전기철도 시스템의 9~150 ㎑ 대역에서의 RFI 노이즈 전달 경로 분석
권석태(Suk-Tai Kwun),정연춘(Yeon-Choon Chung) 한국전자파학회 2012 한국전자파학회논문지 Vol.23 No.12
철도 시스템에서 방사하는 9~150 ㎑ 대역의 자기장 복사 방출은 철도 시스템 주변의 무선 설비 등에 영향을 주어 통신 성능의 저하나 오동작을 초래할 수 있다. 본 논문에서는 전기 철도 시스템에서 방사하는 9~150 ㎑ 주파수 대역의 전자파 노이즈에 대한 등가 회로 모델을 소스 및 전달 경로 분석을 통하여 제안하고, 철도차량의 견인 구동 시스템과 변전 시스템에서 발생하는 수 ㎑의 스위칭 노이즈가 급전선과 선로의 루프 회로를 통하여 방사됨을 확인하였다. 또한, 실제의 구리-국수 간 중앙선 철도의 RC Bank의 효과를 분석하여 이러한 회로 등가 모델의 유효성을 검증하였고, 급전선과 선로 사이에 적정한 용량의 커패시터를 장하함으로써 효과적으로 설계 대책이 가능함을 보였다. The interaction of magnetic field in the frequency range of 9~150 ㎑ radiating from a railway system with wireless systems has been the cause of radio frequency interference. In this paper, the equivalent circuit model of the RFI noise is proposed through source and transfer path analysis, and it is confirmed that the switching noise of several ㎑ that occurs a vehicle traction drive system and a substation is radiated by forming the loop circuit with a feeder line by a rolling stock. And the validity of the proposed equivalent circuit model is verified by analyzing the effects of RC banks installed in the real railway between Guri and Guksu stations, the RFI noise can be effectively mitigated by loading suitable capacitance between rail and feeding line.