http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Bacillus sphaericus 1894 로 부터 새로운 제한효소 Bsp 1894Ⅰ의 분리 및 효소적 특성
류춘제,이청호,유욱준 ( Chun Jehi Ryu,Chung Ho Lee,Ook Joon Yoo ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4
A new restriction endonuclease, Bspl894I, has been isolated from Bacillus sphaericus 1894 (KCTC 1188), and its catalytic properties have been studied. This enzyme recognizes the DNA sequence 5`-G↓GNCC-3` and cleaves at the site as indicated by the arrow. Bsp1894I is an isoschizomer of AsuI, Sau96I, and Cfr13I. It shows maximum activity at a pH range between 6 and 7 in the presence of 10 MM MgCl₂. The optimum reaction temperature for Bsp1894I is 42℃. Unlike its isoschizomers, Bsp1894I does not require NaCl for optimum activity.
A New Restriction Endonuclease, Bsp1894I, from Bacillus sphaericus 1894
류춘제,이청호,유욱준,Ryu, Chun-Jehi,Lee, Chung-Ho,Yoo, Ook-Joon 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4
새로운 제한효소 Bsp1894I을 Bacillus sphaericus 1894(KTCC 1188)로부터 분리하여 그 특성에 대해 연구하였다. Bsp18941은 5'-G${\downarrow}$GNCC-3'를 인식하고 화살표 부위를 절단하며 AsuI, Sau96I, Cfr13I 등과 isoschizomer임을 밝혔다. 또 이 효소는 10 mM $MgCl_2$ 존재하에서 pH 6과 pH 7에서 최대 활성을 보이며 최적온도는 $42^{\circ}C$이고, 위 isoschizomer 들과는 달리 NaCl이 없는 상태에서 정상적인 효소활성을 보여주었다. A new restriction endonuclease, Bsp1894I, has been isolated from Bacillus sphaericus 1894 (KCTC 1188), and its catalytic properties have been studied. This enzyme recognizes the DNA sequence5'-G${\downarrow}$GNCC-3' and cleaves at the site as indicated by the arrow. Bsp1894I is an isoschizomer of AsuI, Sau96I, and Cfr13I. It shows maximum activity at a pH range between 6 and 7 in the presence of 10 MM $MgCl_2$. The optimum reaction temperature for Bsp1894I is $42^{\circ}C$. Unlike its isoschizomers, Bsp1894I does not require NaCl for optimum activity.
Hepatitis B virus preS1에 대한 생쥐 단일클론항체의 제조와 특성연구
김윤규,김희선,류춘제,진병래,홍효정 大韓免疫學會 1996 大韓免疫學會誌 Vol.18 No.3
To generate a murine monoclonal antibody (mAb) to the preSi antigen of hepatitis B virus (HBV), preSi fusion proteins maltose binding protein (MBP)-preSl and glutathione S-transferase (GST)-preSl/preS2 were expressed in Escherichia coli in a soluble form and purified from the cell lysate. Each fusion protein was immunized into BALB/c mice and the resulting antisera were titrated for the antibody to the preSi antigen. The result showed that the immunogenicity of the MBP-preSi was more effective than that of the GST preSi/preS2. Six hybridoma clones secreting good amount of the mAb were isolated and the isotype of each mAb was determined, which showed that two were IgGl and four were IgM. Among them, 1B3 antibody (IgGl), derived from the mice immunized with the MBP-preSi, was purified from the culture supernatant of the hybridoma and characterized. The purified 1B3 bound to the preSi in a dose-dependent manner and immunoprecipitated HBV particles as almost efficiently as anti-S and anti-preS2 mAbs which were previously shown to have the in vitro neutralizing activity for HBV. These results indicate that the MBP-preSl fusion protein can be an useful immunogen for the generation of the anti-preSi murine mAb and the 1B3 mAb may be useful to the fundamental and applied researches related with HBV.