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내산성 Glucoamylase의 정제 및 특성에 관한 연구
김학주,변시명,Kim, Hack-Joo,Byun, Si-Myung 생화학분자생물학회 1977 한국생화학회지 Vol.10 No.3
Paecilomyces subglobosum이 생산하는 내산성 glucoamylase(EC. 3. 2. 1. 3)를 glycogen-Sepharose 4B affinity chromatography에 의하여 1단계 작업으로 정제하였다. Glycogen-Sepharose 4B는 Sepharose 4B를 oxirane으로 activation 시킨후 글리코겐을 결합시켰으며 이 gel은 wet gel g 당 최소한 3.64 units의 glucoamylase를 흡착하였다. 정제한 glucoamylase는 7% polyacryl amide gel 전기영동상에서 단일대를 보여주었다. 정제한 glucoamylase의 Km은 전분과 글리코겐에 대하여 각기 0.154%, 0.125%였으며 이 효소의 최적 pH는 4.0, 최적온도는 $55^{\circ}C$이었다. Glucoamylase는 pH 2에서도 75%의 효소역가를 보여주었고 낮은 pH와 열에 대한 안정성도 비교적 양호하였다. An acid stable glucoamylase from Paecilomyces subglobosum was purified by affinity chromatography using the glycogen-Sepharose 4B gel in the single purification step. Glycogen was coupled to Sepharose 4B by the oxirane activation method and the gel absorbed 3. 64 units of glucoarnylase per gram of wet gel. The purified glucoamylase preparation showed a single protein band on 7% polyacryl amide gel by electrophoresis. Using this purified enzyme some kinetic parameters of the glucoamylase were studied. Km's on starch and glycogen as substrates were 0.154% and 0.125% respectively, the optimal pH 4.0, and the optimal temperature $55^{\circ}C$. The glucoamylase preparation was stable and showed 75% activity even at pH 2.0 and was relatively stable by heat treatment.
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내산성 Glucoamylase 의 정제 및 특성에 관한 연구
김학주,변시명 ( Hack Joo Kim,Si Myung Byun ) 생화학분자생물학회 1977 BMB Reports Vol.10 No.3
An acid stable glucoamylase from Paecilomyces subglobosum was purified by affinity chromatography using the glycogen-Sepharose 4B gel in the single purification step. Glycogen was coupled to Sepharose 4B by the oxirane activation method and the gel absorbed 3.64 units of glucoamylase per gram of wet gel. The purified glucoamylase preparation showed a single protein band on 7% polyacryl amide gel by electrophoresis. Using this purified enzyme some kinetic parameters of the glucoamylase were studied. Km`s on starch and glycogen as substrates were 0.154 % and 0.125% respectively, the optimal pH 4.0, and the optimal temperature 55℃. The glucoamylase preparation was stable and showed 75 % activity even at pH 2.0 and was relatively stable by heat treatment.
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A New Format for Agarose Solid-Phase Enzyme Immunoassay
김학주,양중익,민신홍,변시명,Kim, Hack-Joo,Yang, Jung-Ick,Min, Shin-Hong,Byun, Si-Myung 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.1
B형 간염 표면항원의 모노크로날 항체를 CNBr로 활성화시킨 agarose에 결합시켜 만든 고상 agarose-anti-HBs를 사용하여 측정하고자 하는 시료, 효소결합체, 효소반응을 1회용 플라스틱 주사기에서 이루어지도록 하는 진단방법을 연구하였다. 이 방법으로 실온에서 3시간 이내에 간단한 조작으로 측정이 완료될 수 있었으며 민감도는 기존의 상품화 되어 있는 진단시약과 동일수준을 보여주었고 B형 간염 표면항원 1 ng/ml의 농도를 측정할 수 있었다. A new format for agarose solid-phase enzyme immunosassay (ASEIA) has been developed in which a monoclonal antibody-coupled agarose, packed into a 1-ml disposable plastic syringe, regulates the sample and the enzyme reaction. The assay can be completed in less time at room temperature and in a simpler maner by use of this single-syringe system. The sensitivity of the technique is equivalent to a commercially available enzyme immunoassay kit and was able to detect $1{\mu}g/L$ of hepatitis B surface antigen in this study.
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Rearrangement of Light Chain Gene of Anti-Tac Antibody
김종화,이병룡,김학주,변시명,Kim, Jong-Hwa,Lee, Byeong-Ryong,Kim, Hack-Joo,Byun, Si-Myung 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.3
Anti-Tac 항체를 생산하는 하브리도마 세포인 Hd-2-4-5로 부터 유전자를 분리하고 Bam HI 제한효소를 이용하여 완전 분해한 후 DNA조각을 agarose gel 상에서 크기에 따라 10가지 부분으로 나누였다. 이렇게하여 형성된 각 DNA조각을 Southern blot를 행하므로서 어느 부분이 anti-Tac 항체의 L chain을 가지고 있는지를 확인한 후 in vitro packaging 법과 situ plaque hybridization 방법을 이용하여 L chain을 함유하는 clone을 분리하였다. 이렇게 하여 얻어진 clone으로 부터 pBR 322에 subcloning 실험과 제한효소 지도작성을 통하여 배아세포의 L chain파 비 교함으로써 anti-Tac항체의 L chain의 재배열을 연구했다. 이때 anti-Tac 항체의 L chain은 $J_1-J_2$ cluster가 deletion 되어 있었고 V-J recombination에 의해서 V 부위가 직접 $J_3-J_4-J_5$ cluster에 연결되어 있음을 알 수 있었다. A high molecular weight DNA from a hybridoma cell, Hd-2-4-5, producing anti-tac antibody was digested to completion with BamHI restriction endonuclease. The resulting DNA fragments were fractionated according to the size in 1% preparative agarose gel electrophoresis. After ligation of the fragment with modified Charon 28 and packaging in vitro, DNA fragments carrying the gene sequences coding for the variable region of light chains were detected by hybridization with mouse $J_k$ fragment labeled with $^{32}P$. We have cloned the k-sequence positive BamHI DNA fragments and characterized the cloned sequences by comparing with mouse embryonic light chain. On the basis of the results, it was concluded that the cloned light chain gene underwent somatic rearrangement. The$J_1-J_2$cluster was deleted and the region was directly linked to remaining J cluster by V-J recombination.
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Anti - Tac 항체의 L chain 유전자 재배열
김종화,이병룡,김학주,변시명 ( Jong Hwa Kim,Byeong Ryong Lee,Hack Joo Kim,Si Myung Byun ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.3
A high molecular weight DNA from a hybridoma cell, Hd-2-4-5, producing anti-tac antibody was digested to completion with BamHI restriction endonuclease. The resulting DNA fragments were fractionated according to the size in 1% preparative agarose gel electrophoresis. After ligation of the fragment with modified Charon 28 and packaging in vitro, DNA fragments carrying the gene sequences coding for the varibable region of light chains were detected by hybridization with mouse J_k fragment labeled with ^(32)P. We have cloned the κ-sequence positive BamHI DNA fragments and characterized the cloned sequences by comparing with mouse embryonic light chain. On the basis of the results, it was concluded that the cloned light chain gene underwent somatic rearrangement. The J₁-J₂ cluster was deleted and the region was directly linked to remaining J cluster by V-J recombination.
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고상 Agarose - anti - HBs 결합체를 이용한 B형 간염 표면항원 진단시약
김학주,양중익,민신홍,변시명 ( Hack Joo Kim,Jung Ick Yang,Shin Hong Min,Si Myung Byun ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.1
A new format for agarose solid-phase enzyme immunosassay (ASEIA) has been developed in which a monoclonal antibody-coupled agarose, packed into a 1-ml disposable plastic syringe, regulates the sample and the enzyme reaction. The assay can be completed in less time at room temperature and in a simpler maner by use of this single-syringe system. The sensitivity of the technique is equivalent to a commercially available enzyme immunoassav kit and was able to detect 1 ㎍/L of hepatitis B surface antigen in this study.
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변시명,김학주 한국농화학회 1978 Applied Biological Chemistry (Appl Biol Chem) Vol.21 No.2
Acid-stable α-amylase was partially purified from Paecilomyces subglobosum by Sephadex G-150 gel filtration. About 7.7-fold purification was obtained and the partially purified preparation has 5.0 U of αamylase activity per ㎎ of protein. Using this partially purified α-amylase, general properties were studied and it showed the maximal activities at the conditions of pH 4.0 and 38℃. High stability of the acid-stable α-amylase in acidic condition was observed, whereas thermal stability was similar to the conventional α-amylase.
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