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송기방,김경태,김지영,이상기,한문희,Song, Ki-Bang,Kim, Kyong-Tai,Kim, Ji-Young,Rhee, Sang-Ki,Han, Moon-Hi Korean Society for Biochemistry and Molecular Biol 1987 한국생화학회지 Vol.20 No.2
B형 간염 바이러스 표면항원 유전자가 효모 GAL10, ADCI 혹은 GAL1-ADCI double promoter 조절하에 발현되도록 재조합 플라즈미드를 제조하였다. Double prornoter는 ADCI promoter DNA절편과 GAL1-GAL10 promoter DNA 절편을 결합시킴으로써 만들었다. 효모에서 세가지의 재조합 플라즈미드는 모두 HBsAg을 발현시켰다. GAL promoter가 유도되었을 때 ADCI promoter 보다 3-5 배 많은 HBsAg을 생산하였다. Double promoter 시스템에서 galactose에 의해 전사가 유도되는 것이 확인되었지만 HBsAg 생성량은 유도되기 전의 수준에서 크게 증가되지 않았다. Northern blot에 의해 RNA 분석 결과 윗쪽 GAL promoter 가 유도됨에 따라서 아랫쪽 ADCI promoter 조절하의 전사시작이 저해 되고 있음이 시사되었다. We have constructed plasmids in which transcription of the gene encoding human hepatitis B virus surface antigen(HBsAg) is under the control of GAL10, ADCI or a double promoter consisting of GAL1 and ADCI. Construction of the double promoter was achieved by insertion of a 650 bp fragment of divergent GAL1-GAL10 promoter DNA in the upstream of ADCI promoter. By radioimmunoassay, it was shown that three recombinant plasmids were all capable of producing HBsAg in the host Saccharomyces cerevisiae strains. When induced by galactose, cells synthesized 3-5 fold more HBsAg under GAL promoter control than under ADCI promoter control in an identical plasmid. Production of HBsAg in a system utilizing the double promoter was not increased additively, although it appeared to retain galactose inducibility. Northern blot analysis indicated that induction of the upstream GAL1 promoter caused inhibition of transcription initiation at the downstream ADCI promoter.
GAL1 - ADCI , GAL 10 과 ADCl Promoter 를 이용한 효모에서 B 형 간염 바이러스 표면항원에서 발현
송기방,김경태,김지영,이상기,한문희 ( Ki Bang Song,Kyong Tai Kim,Ji Young Kim,Sang Ki Rhee,Moon Hi Han ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.2
We have constructed plasmids in which transcription of the gene encoding human hepatitis B virus surface antigen(HBsAg) is under the control of GAL10, ADC1 or a double promoter consisting of GAL1 and ADC1. Construction of the double promoter was achieved by insertion of a 650 bp fragment of divergent GAL1-GAL10 promoter DNA in the upstream of ADC1 promoter. By radioimmunoassay, it was shown that three recombinant plasmids were all capable of producing HBsAg in the host Saccharomyces cerevisiae strains. When induced by galactose, cells synthesized 3-5 fold more HBsAg under GAL promoter control than under ADC1 promoter control in an identical plasmid. Production of HBsAg in a system utilizing the double promoter was not increased additively, although it appeared to retain galactose inducibility. Northern blot analysis indicated that induction of the upstream GAL1 promoter caused inhibition of transcription initiation at the downstream ADC1 promoter.
MOLECULAR CLONING OF EXTRACELLULAR LEVANSUCRAE GENE OF ZYMOMNAS MOBILIS ZMIINE. COLI
宋基榜 건국대학교 1992 대학원 학술논문집 Vol.35 No.-
Leven is a fructose polymer of potential importance as fructose source or thickening agent in food industry and plasma expander in pharmaceutical industry. The extracellular levansucrase gene of Zymomonas mobilis ZM1 was cloned in E. coli by shot-gun cloning method. By the analysis of genomic librariesof Z. mobilis ZM1, 13recombinant E. coli colonies showing sucrase activity were obtained. One of these plasmids isolated from these clones was designated as pZL8 and further characterized. The plasmid pZL8 with 4.5Kb Z.mobilis ZM1 chromosomal DNA fragment inserted conferred a sucrase positive phenotype and showed transfructosylation activity(levan-like-polysaccharide formation) in minimal medium, the restriction analysis and deletion experiment revealed that levansucrase gene was included in 2.1Kb DNA fragment, polysaccharide formed in E. doli(pZL8) was identifited as leavan by TLC analysis. Electropholetic behaviour of the levansucrase produced from E. coli(pZL8) was identical to those of the extracellular levansucrase of Z. mobilis ZM1.
Arthrobacter ureafaciens KCTC 3387이 생산하는 InulaseⅡ의 정제 및 특성
이재찬,이기영,송기방,이용복 한국산업미생물학회 1999 한국미생물·생명공학회지 Vol.27 No.6
Arthrobacter ureafaciens KCTC 3387 발효배양상등액으로부터 (NH_4)_2SO_4 침전, DEAE-Toyopearl column chromato-graphy, Sephadex G-200 gel filtration에 의하여 exoinulinase(inulaseⅡ)를 정제하였으며, 정제된 효소의 비활성은 10.49 units/㎎으로, 배양상등액의 7배로 정제되었다. Polyacrylamide gel 전기영동결과 단일 band로 순수하게 분리되었으며 분자량은 45,000으로 추정되었고 Km 값과 V_max 값은 각각 11.9 mM, 3.3 μmol/min/mL 이었다. 효소의 최적반응 pH와 온도는 6.5∼7.0, 55℃이었고, pH는 4.0∼10.6, 온도는 60℃까지 안정하였다. 대부분의 금속이온은 효소활성에 거의 영향을 미치지 않았으나 Hg^2+ 이온에 의해 효소활성이 크게 저해를 받았고, 금속이온으로 열처리한 효소의 경우 Ag^+, Hg^2+, Fe^2+ 와 Hg^2+ 에 의해 저해를 받았다. Inulin을 24시간 분해한 후의 반응산물은 DFAⅢ, GF_2 및 GF_3 이었다. 이것은 효소가 GF_2 와 GF_3를 기질로 이용하지 못함을 나타내는데 반하여 기질에 대한 효소반응결과 GF_3는 sucrose와 DFAⅢ를, GF_2도 미량의 DFAⅢ 를 생산하는 것으로 볼 때 기질에 따른 특성으로 보인다. Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseⅡ) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAⅢ) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650 M and gel filtration on Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH 6.5∼7.0 and 55℃, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to 60℃. The K_m of this enzyme for DFAⅢ production was 11.9 mM. The enzyme was inactivated by Hg^2+ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition to DFAⅢ.
된장으로 부터 fibrin 용해 세균의 분리에 관한 연구
이시경,주현규,송기방,허석 한국농화학회 1999 Applied Biological Chemistry (Appl Biol Chem) Vol.42 No.1
The bacteria which could hydrolyze the fibrin produced through the blood coagulation mechanism in the human body, were isolated from soybean paste. The KDO-13 strain was selected among the isolated bacteria as the best strain for fibrinolytic activity. It was spore forming and Gram positive. C_(15:0) anteiso fatty acid, C_(15:0) iso fatty acid and C_(15:0) anteiso fatty acid were 47.7, 13.5 and 13.6%, respectively as major component among its cellular fatty acid composition. It showed the similarity of 57.7%, compared with standard strain. It was thus identified to be Bacillus atrophaeus according to Bergey's manual of systematic bacteriology and its fatty acid profiles of gas chromatography. The optimum culture temperature and pH were 37℃ and 6 for the production of fibrinolytic enzyme by Bacillus atrophaeus KDO-13.
이재찬,이기영,송기방,이용복 전남대학교 약품개발연구소 2000 약품개발연구지 Vol.9 No.1
For thee mess production of DFAIII and for the development of techniques of separation and purification of it. the methods of production of DFAIII and its recovery was investigated by fermentation win, the strain of Arthrobacter ureafaciens KCTC 3387 and by enzyme reaction. In the first method, DFAIII was produced by fermentation with the strain of Arthrobacter ureafaciens KCTC 3387 and recovered from culture supernatant with silica gel by gel filtreation, in the second method, it was produced by enzyme reaction and recovered with the same method of the Brat, and in the third method it was produced by fermentation and recovered by addition of ethanol to the culture supernatnat. Against 25 g/L of initial concentration of inulin, 1.57, 4.40, 0.34 g/L of powder of DFAIII was recovered respectively and the rate of recovery wins 6.3, 17.6, 1.4% and the purity was estimated at 81, 97, 87% respective. For the production of DFAIII and its recovery, enzyme reaction method was the twin the rate of recovery and its purity. By fermentation method, DFAIII was produced with 50% of initial concentration of substrate the rate of recovery was lower than enzyme reaction method and purity was lowest among the three methods. Ethanol pricipitation method showed the lowest rate of recovery.