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서로 다른 트래픽을 가진 ATM 멀티플렉서의 셀손실율 분석
전원구,음호식 공주영상정보대학 2000 논문집 Vol.7 No.-
ATM 멀티플렉서에서의 셀손실율은 우선순위를 부여 하였을 경우에, 손실 우선순위 제어 파리미터가 0.75이하 일 때는 낮은 우선순위의 셀손실율에 의해서 연결 수락이 결정되고 0.9일 때는 높은 우선순위의 셀손실율에 의해 연결 수락이 결정됨을 알 수 있었다. 셀손실율은 입력 소스의 수가 증가함에 따라, 셀손실율도 함께 증가하였고 버스트성과도 비례함을 알 수 있었다. 전체 버퍼의 수를 고정시키고 한계 버퍼의 수를 증가시키면, 한계 버퍼 안에서는 낮은 우선순위의 셀이 더 많이 저장됨을 알 수 있었다. 높은 우선순위의 셀은 버퍼의 크기에 영향을 받지만 낮은 우선순위의 셀손실율은 버퍼의 크기와는 무관하게 임계 버퍼값에 영향 받음을 알 수 있었다. 그러므로 낮은 우선순위의 셀손실율에 의하여 연결 수락 제어가 결정됨을 알 수 있으며, 연결 수락 제어에 의해 연결된 소스는 파라미터와 한계 버퍼의 크기 L에 의해서 영향받음을 알 수 있었다. 따라서, ATM 멀티플렉서의 통계적 다중화 이득을 증가하기 위해서, 손실 우선순위 제어를 이용하는 것이 유리하다.
김선문,허원석,채경훈,강윤세,정재훈,김연수,박기오,문희석,이엄석,김석현,성재규,이병석,이헌영,신경숙,조준식,송인상,강대영 충남대학교 의학연구소 2003 충남의대잡지 Vol.30 No.2
Malignant peritoneal mesothelioma is a rare neoplasm that arises from the mesothelium of a serosal cavity and is a rapidly fatal disease with a median survival of 4 to 12 months for untreated cases. Recently, we experienced a case with malignant peritoneal mesothelioma who was suspected hepatocelluar carcioma by abdominal CT scan and was confirmed by biopsy including immunohistochemical stain(calretinin) after surgery. We performed tumor excisions and wedge resection of the liver(segment Ⅷ)and inserted Tencoff catheter in abdominal cavity at 25th day of post-operation. We treated with intraperitoneal paclitaxel(25mg/m^(2)/day for 5 days) six courses monthly. She was well tolerable and is still living without any evidence of recurrence for 14th month of post-operation.
Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin
Eum, Won-Sik,Choi, Hee-Soon,Kim, Dae-Won,Jang, Sang-Ho,Choi, Soo-Hyun,Kim, So-Young,Park, Jin-Seu,Kang, Jung-Hoon,Cho, Sung-Woo,Kwon, Oh-Shin,Hwang, In-Koo,Yoo, Ki-Yeon,Kang, Tae-Cheon,Won, Moo-Ho,Cho Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.1
Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. Monoclonal antibodies (mAbs) against human CP were produced and characterized. A total of five hybridoma cell lines were established (CP2, CP10, CP20, CP25, CP30). From the epitope mapping analysis, two subgroups of mAbs recognize different peptide fragments were identified. When the purified CP was incubated with the mAbs, the ferroxidase activity of CP was inhibited up to a maximum 57%. Immunoblotting with various tissue homogenates indicated that all the mAbs specifically recognize a single protein band of 130 kDa. They also appear to be extensively cross-reactive among different mammalian including human and avian sources. These results demonstrated that only one type of immunologically similar CP is present in all of the mammalian tissues including human. The CP mAbs could be of great benefit to design the diagnostic kit for CP-related diseases such as Wilson's disease.
Eum, Won Sik,Shin, Min Jea,Lee, Chi Hern,Yeo, Hyeon Ji,Yeo, Eun Ji,Choi, Yeon Joo,Kwon, Hyun Jung,Kim, Duk-Soo,Kwon, Oh Shin,Lee, Keun Wook,Han, Kyu Hyung,Park, Jinseu,Kim, Dae Won,Choi, Soo Young Elsevier 2019 Biochimie Vol.156 No.-
<P><B>Abstract</B></P> <P>Parkinson's disease (PD), a neurodegenerative disorder, is characterized by a loss of dopaminergic neurons in the substantia nigra (SN) of the brain and it is well known that the pathogenesis of PD is related to a number of risk factors including oxidative stress. Antioxidant 1 (ATOX1) protein plays a crucial role in various diseases as an antioxidant and chaperone. In this study, we determined whether Tat-ATOX1 could protect against 1-methyl-4-phenylpyridinium ion (MPP<SUP>+</SUP>)-induced SH-SY5Y cell death and in a 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced animal model of PD. In the MPP<SUP>+</SUP> exposed SH-SY5Y cells, Tat-ATOX1 markedly inhibited cell death and toxicities. In addition, Tat-ATOX1 markedly suppressed the activation of Akt and mitogen activated protein kinases (MAPKs) as well as cleavage of caspase-3 and Bax expression levels. In a MPTP-induced animal model, Tat-ATOX1 transduced into brain and protected dopaminergic neuronal cell loss. Taken together, Tat-ATOX1 inhibits dopaminergic neuronal death through the suppression of MAPKs and apoptotic signal pathways. Thus, Tat-ATOX1 represents a potential therapeutic protein drug candidate for PD.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Tat-ATOX1 transduces into SH-SY5Y cells and inhibited MPP<SUP>+</SUP>-induced cell death. </LI> <LI> Tat-ATOX1 suppressed the activation of Akt and MAPKs in MPP<SUP>+</SUP> exposed SH-SY5Y cells. </LI> <LI> Tat-ATOX1 inhibited dopaminergic neuronal cell loss in MPTP-induced animal model. </LI> <LI> Tat-ATOX1 represent a potential therapeutic agent for PD. </LI> </UL> </P>
Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin
( Won Sik Eum ),( Hee Soon Choi ),( Dae Won Kim ),( Sang Ho Jang ),( Soo Hyun Choi ),( So Young Kim ),( Jin Seu Park ),( Jung Hoon Kang ),( Sung Woo Cho ),( Oh Shin Kwon ),( In Koo Hwang ),( Ki Yeon Y 생화학분자생물학회 2005 BMB Reports Vol.38 No.1
Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. Monoclonal antibodies (mAbs) against human CP were produced and characterized. A total of five hybridoma cell lines were established (CP2, CP10, CP20, CP25, CP30). From the epitope mapping analysis, two subgroups of mAbs recognize different peptide fragments were identified. When the purified CP was incubated with the mAbs, the ferroxidase activity of CP was inhibited up to a maximum 57%. Immunoblotting with various tissue homogenates indicated that all the mAbs specifically recognize a single protein band of 130 kDa. They also appear to be extensively cross-reactive among different mammalian including human and avian sources. These results demonstrated that only one type of immunologically similar CP is present in all of the mammalian tissues including human. The CP mAbs could be of great benefit to design the diagnostic kit for CP-related diseases such as Wilson`s disease.
Hydroxyl Radical-Generating Function of Horseradish Cu,Zn-Superoxide Dismutase
Eum, Won-Sik,Kwon, Oh-Bin,Kang, Jung Hoon Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.5
Cu,Zn-superoxide dismutase (SOD) was purified from horseradish by using Mono Q and Superose 12 FPLC column chromatography. The native molecular mass of the purified enzyme was approximately 33 kDa, as determined by gel filtration. The subunit molecular weight, as estimated by SDS-PAGE, was 16 kDa. These results indicated that the native enzyme is a homodimer. We investigated the free radical-generating function of horseradish Cu,Zn-SOD by using a chromogen, 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) which reacts with ${\cdot}OH$ radicals to form $ABTS^{+{\cdot}}$ The formation of $ABTS^{+{\cdot}}$ was required for both active Cu, Zn-SOD and $H_2O_2$. The optimal pH for the free radical-generating activity of this enzyme was 6.0-8.0, and it retained about $40^{\circ}C$ of its maximum activity when exposed at $40^{\circ}C$ for 15 min. A neutral scavenger, ethanol, inhibited the $ABTS^{+{\cdot}}$ formation by horseradish Cu, Zn-SOD more effectively than that by the mammalian enzyme. These results suggest that the active channel of horseradish enzyme is slightly larger than that of the mammalian enzyme.
Eum, Won Sik,Jang, Sang Ho,Kim, Dae Won,Choi, Hee Soon,Choi, Soo Hyun,Kim, So Young,An, Jae Jin,Lee, Sun Hwa,Han, Kyuhyung,Kang, Jung Hoon,Kang, Tae-Cheon,Won, Moo Ho,Cho, Yong Joon,Choi, Jin Hi,Kim, Korean Society for Molecular Biology 2005 Molecules and cells Vol.19 No.2
<P>The human immunodeficiency virus type 1 (HIV-1) Tat protein transduction domain (PTD) is responsible for highly efficient protein transduction across plasma membranes. In a previous study, we showed that Tat-Cu,Zn-superoxide dismutase (Tat-SOD) can be directly transduced into mammalian cells across the lipid membrane barrier. In this study, we fused the human SOD gene with a Tat PTD transduction vector at its N- and/or C-terminus. The fusion proteins (Tat-SOD, SOD-Tat, Tat-SOD-Tat) were purified from Escherichia coli and their ability to enter cells in vitro and in vivo compared by Western blotting and immunohistochemistry. The transduction efficiencies and biological activities of the SOD fusion protein with the Tat PTD at either terminus were equivalent and lower than the fusion protein with the Tat PTD at both termini. The availability of a more efficient SOD fusion protein provides a powerful vehicle for therapy in human diseases related to this anti-oxidant enzyme and to reactive oxygen species.</P>