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L5178Y 동물 배양세포에 있어서 Tubercidin 의 세포독성과 핵산합성에 미치는 영향
조중명,이세영 ( Jung Myung Cho,Se Yong Lee ) 생화학분자생물학회 1978 BMB Reports Vol.11 No.2
Tubercidin is an adenosine analogue (7-deazaadenosine) which was highly cytotoxic to L5178Y murine leukemia cells in culture. Its effective range of cytocidal concentration was extremely narrow. Treatment of 0.3㎍/㎖ tubercidin for 2 hrs. led to 90-95% cell kill. Tubercidin at lower concentrations inhibited RNA synthesis slightly more than DNA synthesis in L5178Y cells. The effects of tubercidin on ³H-adenosine and ³H-uridine incorporation to nucleic acids were very similar, indicating that its action is not at the transport or adenosine kinase sites. Our results showed that ribosmal RNA and nucleolar RNA were most sensitive to tubercidin. However, they were not completely inhibited by the cytotoxic concentration. Synthesis of messenger RNA was less sensitive to the drug than ribosomal RNA. Transfer RNA and other small cytoplasmic RNA were not inhibited by even higher concentrations. The sensitivity of messenger RNA with or without the poly (A) segments to tubercidin was indifferent. The combination of tubercidin with another antineopleastic RNA inhibitor, actinomycin D, did not exhibited a synergistic effect on RNA synthesis in L5178Y cells.
L5178Y 동물 배양세포에 있어서 Tubercidin의 세포독성과 핵산합성에 미치는 영향
조중명,이세영,Cho, Jung-Myung,Lee, Se-Yong 생화학분자생물학회 1978 한국생화학회지 Vol.11 No.2
동물 암세포에서 항암작용을 나타내는 adenosine 유사체 항생제 Tubercidin을 배양중에 있는 생쥐의 임파종양 L5178Y세포에 처리하여 그의 세포독성과 핵산합성에 미치는 영향을 조사한 결과 다음과 같은 결론을 얻었다. 1) $0.3{\mu}g/ml$의 농도로 2 시간 처리했을때 약 90~95%의 세포치사가 일어났다. 2) DNA 합성보다는 RNA 합성은 약간 더 저해 하였다. 3) 여러가지 RNA 종류에 미치는 영향을 조사한 결과 각 RNA 종류에 대한 특이성은 뚜렷하지 않았으나 메센저 RNA 보다는 리보좀 RNA 합성을 보다 더 예민하게 저해하였는데, 이때 transfer RNA를 포함한 작은 크기의 세포질 RNA 합성에는 별로 영향을 미치지 않았다. 또한 메센저 RNA중에서 poly(A) 사슬을 지닌 poly(A)-mRNA에 선택적으로 영향을 미치지는 않았다. RNA에 대한 tubercidin의 작용은 RNA 합성에 직접영향을 미치는 것이며, RNA의 수송에 관여하는 것이 아니라는 사실을 알았다. 4) 리보좀 RNA 합성을 선택적으로 저해하는 또 하나의 항암제인 actinomycin D와 tubercidin과의 병합처리가 RNA의 합성저해에 상승효과를 나타 내지는 않았고 합산효과를 나타 내었다. Tubercidin is an adenosine analogue (7-deazaadenosine) which was highly cytotoxic to L5178Y murine leukemia cells in culture. Its effective range of cytocidal concentration was extremely narrow. Treatment of $0.3{\mu}g/ml$ tubercidin for 2 hrs. led to 90-95% cell kill. Tubercidin at lower concentrations inhibited RNA synthesis slightly more than DNA synthesis in L5178Y cells. The effects of tubercidin on $^3H$-adenosine and $^3H$-uridine incorporation to nucleic acids were very similar, indicating that its action is not at the transport or adenosine kinase sites. Our results showed that ribosmal RNA and nucleolar RNA were most sensitive to tubercidin. However, they were not completely inhibited by the cytotoxic concentration. Synthesis of messenger RNA was less sensitive to the drug than ribosomal RNA. Transfer RNA and other small cytoplasmic RNA were not inhibited by even higher concentrations. The sensitivity of messenger RNA with or without the poly (A) segments to tubercidin was indifferent. The combination of tubercidin with another antineopleastic RNA inhibitor, actinomycin D, did not exhibited a synergistic effect on RNA synthesis in L5178Y cells.
정혜신,조중명 ( Hye - Shin Chung Park,Joong Myung Cho ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.3
Native monellin, an intensely sweet protein from a tropical plant, consists of two chains, A and B chains. The crystal structure of native monellin has been solved at low resolution. Single chain monellin, PS1 has been produced by genetic method. We have done 100 ps molecular dynamics studies of the two chain protein in order to obtain initial coordinates for the B-A fused monellin, PS1. Fifteen sets of coordinates from the dynamics trajectory were picked. Two chains were connected by a peptide bond and minimized each. One of fifteen minimized PS1 contains cis-peptide in the fusion loop. In addition, loop search to find the protein fragments from the well-defined structures which fit the C alpha atomic positions of nearby beta-strands results in several fragments containing cis-Pro. The informations from the present studies are useful in designing the fusion loop of monellin to increase the themostability.
Saccharomyces cerevisiae에서 발현된 유전자 재조합 인 성장 호르몬 생리활성도 측정
원특연,조중명,정경훈,이관우,박순재,김범수 대한내분비학회 1990 Endocrinology and metabolism Vol.5 No.3
The gene for recombinant human growth hormone (rHGH) was constructed and then overexpressed in yeast, Saccharomyces cerevisiae. The protein was purified by successive chromatography processes and purity was more than 98.5% as assessed by SDS-PAGE. The reverse-phase HPLC pattern of the purified rHGH showed that the protein eluted as a single entity from the column, regradless of the mobile phases used. The secondary structure of rHGH determined by circular dichroism spectrophotometer indicated that the -helical content represented about 55% of total protein. The weight gain in hypophysectomized rats, observed during 15 days, as a result of daily injections (125 mIU) of natural human growth hormone standard. The injection of a larger amount of rHGH (200 g) increased weight-gain even more substantially. The efficacy of rHGH determined by radioreceptor assay was slightly better than that of natural human growth hormone standard. (J Kor Soc Endocrinol 5:198~205, 1990)
우성균,백성희,신동훈,김혜선,유영준,조중명,강만식,정진하,U, Seong-Gyun,Baek, Seong-Hui,Sin, Dong-Hun,Kim, Hye-Seon,Yu, Yeong-Jun,Jo, Jung-Myeong,Gang, Man-Sik,Jeong, Jin-Ha The Korean Society for Integrative Biology 1997 Korean journal of biological sciences Vol.1 No.2
We have previously shown that chick muscle extracts contained at least 10 different ubiquitin C-terminal hydrolases (UCHs). In the present studies, one of the enzymes, called UCH-9, was purified by conventional chromatographic procedures using $^{125}l$-labeled ubiquitin-${\alpha}$NH-MHISPPEPESEEEEE HYC (Ub-PESTc) as a substrate. The purified enzyme behaved as a 27-kDa protein under both denaturing and nondenaturing conditions, suggesting that it consists of a single polypeptide chain. It was maximally active at pHs between 7 and 8.5, but showed little or no activity at pH below 6 and above 10. Lice other UCHs, its activity was strongly inhibited by sulfhydryl blocking reagents, such as iodoacetamide, and by Ub-aldehyde. In addition to Ub-PESTc, UCH-9 hydrolyzed Ub-aNH-protein extensions, including Ub-${\alpha}NH$-carboxyl extension protein of 80 amino acids and Ubo-${\alpha}NH$-dihydrofolate reductase. However, this enzyme was not capable of generating free Ub from mono-Ub-${\varepsilon}NH$-protein conjugates and from branched poly-Ub chains that are ligated to proteins through ${\varepsilon}NH$-isopeptide bonds. This enzyme neither could hydrolyze poly-His-tagged di-Ub. These results suggest that UCH-9 may play an important role in production of free Ub and ribosomal proteins from their conjugates.