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한국형 사람 Caliciviruses의 RNA - Dependent RNA Polymerase Diversity
한동표,김지애,양재명,김경희 대한바이러스학회 1997 Journal of Bacteriology and Virology Vol.27 No.1
Human caliciviruses (HuCVs) cause sporadic cases and outbreaks of acute gastroenteritis (AGE). Three major genogroups of HuCVs have been described including the Norwalk virus (NV)-, the Snow Mountain virus (SMA)-, and the Sapporo-genogroups. This study describes the detection and genetic variation of HuCVs from hospitalized infants with AGE in Korea by RT- PCR and sequencing. The cDNA fragments of 206 to 470bp corresponding to the region of 3 primer pairs (36/35, 35/51 or 3/51) in the polymerase region of NV were generated. Of 185 stools screened, 8% were positive by RT-PCR and their sequences showed that all strains contained the GLPSG and YGDD motifs which are conserved for HuCVs. Amino acid (aa) sequence analysis showed that these strains can be divided into 3 major genogroups. High conservation was observed in that one strain shares 100% of aa sequence with Southampton virus, another shares 99% with the Sapporo virus, and six strains share 90 to 95% with Snow Mountain virus. However, significant sequence variation was also found in other strains. This study indicates that all major genogroups of HuCVs are circulating in Korea.
Cellulomonas sp . ATCC 21399에서 Cellulase 분리 및 그 특성
한동표,김택영 ( Dong Pyou Han,Taik Yung Kim ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.3
Cellulomonas sp. ATCC 21399 contained at least 9 components with carboxylmethyl cellulase (CMCase) activity determined by non-denaturing polyacrylamide gel electrophoresis (PAGE). One of the active components was purified through ammonium sulfate fractionation, Sephadex G-150 gel filtration chromatography, and DEAE-Sephadex A-25 ion exchange chromatography. The degree of purification of the enzyme was determined by PAGE and SDS-PAGE. The enzyme was glycosylated, and its molecular weight was estimated to be about 64,000 in SDS-PAGE. The optimum temperature for the enzyme was about 55℃. The enzyme activity was optimum at pH 5.5, and was constant from pH 7.0 to 8.5. Thermalstability studies showed that the enzyme was completely inactivated after 2×(1/2) hour incubation at 60℃, and 4 hour incubation at 55℃. But the enzyme was stable after 6 hour incubation at 50℃.
Isolation and Characterization of a Cellulase from Cellulomonas sp. ATCC 21399
한동표,김택영,Han, Dong-Pyou,Kim, Taik-Yung 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.3
Cellulomonas sp. ATCC 21399는 carboxymethyl cellulase (CMCase) activity를 가지는 성분을 분비하는데 이 cellulase activity는 nondenaturing polyacrylamide gel electrophoresis (PAGE) 법과 CMC agar replica 법을 이용, 측정하여 9가지의 성분으로 분리 확인되었다. 이들 중 한 성분을 ammonium sulfate 분획분리, Sephadex G-150 gel filtration 크로마토그라피, DEAE-Sephadex A-25 이온교환 크로마토그라피 방법 등으로 분리 정제하였다. 효소의 정제 정도는 PAGE와 SDS-PAGE 방법을 이용하여 확인하였다. 이 효소는 당단백질이며 분자량이 약 64,000으로 추정되었다. 이 효소의 활성도가 최적인 온도는 $55^{\circ}C$이고, 최적 pH는 5.5로 밝혀졌고 pH 7.0에서 8.5 사이에는 활성도에 변화는 주지 않음이 밝혀졌다. 열 안정성 조사에서 이 효소률 $60^{\circ}C$에서 $2\frac{1}{2}$ 시간동안 열처리 시키면 활성도를 완전히 상설하지만 $55^{\circ}C$에서는 4시간동안 열처리 시켜야 활성도가 완전히 사라졌다. 그러나 $50^{\circ}C$에서 6시간동안열처리에서도 매우 안정했다. Cellulomonas sp. ATCC 21399 contained at least 9 components with carboxylmethyl cellulase (CMCase) activity determined by non-denaturing polyacrylamide gel electrophoresis (PAGE). One of the active components was purified through ammonium sulfate fractionation, Sephadex G-150 gel filtration chromatography, and DEAE-Sephadex A-25 ion exchange chromatography. The degree of purification of the enzyme was determined by PAGE and SDS-PAGE. The enzyme was glycosylated, and its molecular weight was estimated to be about 64,000 in SDS-PAGE. The optimum temperature for the enzyme was about $55^{\circ}C$. The enzyme activity was optimum at pH 5.5, and was constant from pH 7.0 to 8.5. Thermalstability studies showed that the enzyme was completely inactivated after $2\frac{1}{2}$ hour incubation at $60^{\circ}C$, and 4 hour incubation at $55^{\circ}C$. But the enzyme was stable after 6 hour incubation at $50^{\circ}C$.
한국형 C형 간염 바이러스의 NS5 지역 cDNA 클로닝과 발현
한동표,이택열,김원배,김병문,장미윤,양재명 대한바이러스학회 1997 Journal of Bacteriology and Virology Vol.27 No.2
Three cDNA fragments located within NSS region of HCV were synthesized by RT using viral RNA extracted from blood sample of Korean patient as a template. The cDNAs were amplified by PCR, cloned into the T-vector, and the nucleotide sequences were determined. Comparative analysis of the nucleotide and amino acid sequence of NSS cDNAs showed that it is closely related with HCV type 1b. The cloned NSS cDNA showed 91-94% homology at the nucleotide sequence level and 96-98% homology at the amino acid sequence level with several strains of the HCV type lb. The NS5 cDNAs were subcloned into E. coli expression vectors to construct pRSETA5-1, pTHAN5-1, pRSETC5-2, pRSETBB1, pRESTCB1 and pRSETB-H3. Expression of the NSS proteins was achieved by inducing the promoter with isopropyl-thio-p-D- galactoside (IPTG) and confirmed by SDS-polyacrylamide gel electrophoresis. The NSS proteins were immunoreactive against sera from Korean hepatitis C patients in Western blot analysis. Among the recombinant NSS proteins, pRSETA5-1 plasmid derived protein, coded from aa2022 to aa2521 of HCV polyprotein, showed the strongest immunoreactivity against sera from Korean hepatitis C patients in immunoblot analysis. These results suggest that NSS proteins would be useful as an antigen for detection of antibody against HCV in the blood samples.