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- 저자 : J. Alimaa (검색결과 3 건)
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( Oidov Baatarkhuu ),( N Tuvshinjargal ),( T Alimaa ),( B Tsatsralt Od ),( J Amarsanaa ),( H Okamoto ) 대한간학회 2013 춘·추계 학술대회 (KASL) Vol.2013 No.1
Background/aims: Mongolia is known for its high endemicity for HBV, HCV, and HDV infections among apparently healthy populations. However there are little or no data on the prevalence and genotype distribution of HBV, HCV and HDV among patients with chronic liver diseases in Mongolia. Materials and methods: Serum samples obtained in 2009 from 207 patients (51.0±1.9 years) including those chronic hepatitis (n=90), liver cirrhosis (n=41), and HCC (n=76) were tested for serological and molecular markers of HBV, HCV, and HDV infections. Results: Of the 207 patients, 144 (69.6%), 106 (51.2%), and 117 (56.5%) tested positive for HBsAg and HBV DNA , HCV RNA, and HDV RNA, respectively. Collectively, 172 patients (83.1%) were viremic for one or more of these viruses, including dual viremia of HBV/HDV (26.6%) or HBV/HCV (7.7%) and triple HBV/HCV/HDV viremia (30.0%). Of note, triple ongoing infection was significantly more frequent among patients with HCC than among those with chronic hepatitis (63.2%) vs. 14.4%, P≤0.0001). The distribution of HBV genotypes among the 116 HBV-viremic patients was: A (0.9%), B (0.9%), C (6.0%), D (88.8%), and C plus D(3.4%). All 117 HDV isolates were classified into genotype 1. The 106 HCV RNA positive samples were typed as genotype 1b (92.5%). Conclusions: The present study revealed that ongoing dual or triple infection of HBV, HCV and HDV is highly prevalent among patients with chronic liver diseases of Mongolia.
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Purification and Characterization of Mongolian Mare Lactoferrin
김기성,Ji-Sun Kim,신미순,Hae-Won Noh,임상동,Duvjir Suvd,J. Alimaa 한국축산식품학회 2009 한국축산식품학회지 Vol.29 No.2
The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopearl-AF-Heparin-650M) in two steps. Mare lactoferrin-containing fractions were identified in the first peak among 3 peaks on Sephadex G-100 as first step, and purified lactoferrin was eluted with a step gradient of 0.5 M NaCl as a 3 step (gradient 0.1, 0.3, 0.5M). Eluted fractions were analyzed by 12% SDS-PAGE, and showed a single protein. Its molecular weight was estimated to be 82 kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEXAKXA. The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopearl-AF-Heparin-650M) in two steps. Mare lactoferrin-containing fractions were identified in the first peak among 3 peaks on Sephadex G-100 as first step, and purified lactoferrin was eluted with a step gradient of 0.5 M NaCl as a 3 step (gradient 0.1, 0.3, 0.5M). Eluted fractions were analyzed by 12% SDS-PAGE, and showed a single protein. Its molecular weight was estimated to be 82 kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEXAKXA.
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Purification and Characterization of Mongolian Mare Lactoferrin
Kim, Kee-Sung,Kim, Ji-Sun,Shin, Mi-Soon,Noh, Hae-Won,Lim, Sang-Dong,Suvd, Duvjir,Alimaa, J. Korean Society for Food Science of Animal Resource 2009 한국축산식품학회지 Vol.29 No.2
The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopear1-AF-Heparin-650M) in two steps. Mare lactoferrin-containing fractions were identified in the first peak among 3 peaks on Sephadex G-100 as first step, and purified lactoferrin was eluted with a step gradient of 0.5M NaCl as a 3 step (gradient 0.1,0.3, 0.5M). Eluted fractions were analyzed by 12% SDS-PAGE, and showed a single protein. Its molecular weight was estimated to be 82kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEXAKXA.
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