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KWON, SANGHOON,KIM, DONGBUM,PARK, BYOUNG KWON,WU, GUANG,PARK, MIN CHUL,HA, YANG-WHA,KWON, HYUNG-JOO,LEE, YOUNGHEE Spandidos Publications 2013 Oncology reports Vol.29 No.2
<P>The innovation of a peptide vaccine strategy may contribute to the development of efficacious and convenient cancer vaccines. Recently, we formulated an efficacious peptide vaccine without carriers using the natural phosphodiester bond CpG-DNA and a special liposome complex [Lipoplex(O)]. The peptide vaccine targeting a tumor antigen, transmembrane 4 superfamily member 5 protein (TM4SF5), was confirmed to have preventive and therapeutic effects in a mouse hepatocellular carcinoma (HCC) model. In this study, we demonstrated that the isotype-switched (IgM(-)IgD(-)) B cell population increased after immunization and that the functional memory response persisted for at least 70 days after the final immunization of mice. Delayed implantation of BNL-HCC cells significantly induced the peptide-specific IgG2a production in the immunized mice. Accordingly, tumor growth was inhibited and the survival rate increased. These results suggest that our peptide vaccine induces memory response, which is essential for cancer vaccine application.</P>
Properties of the Endonuclease Secreted by Human B Lymphoblastic IM9 Cells
Kwon, Hyung-Joo,Kim, Doo-Sik Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.1
We have employed a DNA-native-polyacrylamide gel electrophoresis (DNA-native-PAGE) assay system to characterize the enzyme activity of the endonuclease secreted by human B lymphoblastic IM9 cells. Experimental results clearly demonstrated that the endonuclease activity of IM9 cell culture medium is distinct from that of DNase I in the DNA-native-PAGE assay system. Immunoprecipitation analysis using anti-DNase I antibody showed that the secreted endonuclease is not recognized by the antibody. The secreted endonuclease was estimated using supercoiled plasmid DNA as a substrate. The pH optimum required for the catalytic activity was determined to be in the range of pH 6.6-7.4. No significant difference in the endonuclease secretion was observed by stimulation of the IM9 cells with interferon-${\gamma}$ or interleukin-$1{\beta}$.
Properties of the Endonuclease Secreted by Human B Lymphoblastic IM9 Cells
( Hyung Joo Kwon,Doo Sik Kim 생화학분자생물학회 1998 BMB Reports Vol.31 No.1
We have employed a DNA-native-polyacrylamide gel electrophoresis (DNA-native-PAGE) assay system to characterize the enzyme activity of the endonuclease secreted bv human B lymphoblastic IM9 cells. Experimental results clearly demonstrated that the endonuclease activity of IM9 cell culture medium is distinct from that of DNase I in the DNA-native-PAGE assay system. Immunoprecipitation analysis using anti-DNase I antibody showed that the secreted endonuclease is not recognized by the antibody. The secreted endonuclease was isolated from the cell culture medium by native-PAGE elution technique, and the enzyme activity was estimated using supercoiled plasmid DNA as a substrate. The pH optimum required for the catalytic activity was determined to be in the range of pH 6.6-7.4. No significant difference in the endonuclease secretion was observed by stimulation of the IM9 cells with interferon-γ or interleukin-1β.