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Acid Stable Trypsin Inhlbitor 에 대한 단일클론 항체의 제조와 위암조직에서의 발현양상
유욱준,정연태,문형배,김정중,이황희,장원희,노종섭,최완성 한국유전학회 1994 Genes & Genomics Vol.16 No.4
Monoclonal antibodies against human acid stable trypsin inhibitor (ASTI) was produced by hybridizing SP2/0-Ag14 mouse myeloma cells with spleen cells of Balb/c mouse immunized with ASTI. Western blotting analysis using purified ASTI and urinary proteins exhibited the specificity of the antibodies agains ASTI. The distribution and localization of ASTI in adenocarcinoma of stomach were examined using immunohistochemical techniques. ASTI immunoreactivity was detected from the tubular adenocarcinoma, but not from the signet ring cell carcinoma or mucinous adenocarcinoma.
유욱준 한국미생물학회 1988 微生物과 産業 Vol.14 No.1
본 장의 주제인 재조합 유전자의 발현 증대를 위하여는 우리가 알고 있는 대부분의 생명현상에 대한 지식들이 응용될수 있을 것으로 일단 믿어진다. 그러나 그 지식들은 하나의 장으로 모아지기에는 너무나 방대하며 또한 그 각각의 지식들을 어떻게 서로 조화시켜 유전자 발현증대를 꾀할 것이냐 하는 것은 상당한 노력이 더 필요할 것이다. 여기에서는 이미 그 응용이 가능하였던 내용들을 기초로하여 유전자 발현조절에 대하여 알고 있는 지식들을 어떻게 재조합 유전자 실험에 응용하여 그 발현증대를 시도할 수 있겠는가에 대하여 기술해 보고자 한다.
Researches on Restriction - Modification Enzymes
유욱준 한국유전학회 1986 Genes & Genomics Vol.8 No.1
1. Large scale preparation of Stu I endonuclease One million units of homogeneous Stu I endonuclease have been isolated from 100g (wet weight) of Streptomyces tubercidicus cells. For the purification of this enzyme, DEAE-Sephadex (A-50), QAE-Sephadex (A-50) and Heparin-Agarose column chromatography have been performed after ammonium sulfate fractionation of the crude extract. The subunit molecular weight was 34,000 dalton as judged by 10% SDS-polyacrylamide gel electrophoresis. Stu I endonuclease requires Mg^(2+) for its activity and shows maximum activity at pH 7.0-8.0 in the absence of NaCl. 2. Zan I endonuclease: An Isoschizomer of Eco RII and Bst NI endonuclease A new sequence specific endonuclease, Zan I endonuclease, from Zymomonas anaerobia has been purified to homogeneity. The subunit molecular weight was 31,000 dalton as judged by 10% SDS-polyacrylamide gel electrophoresis. The endonucleolytic cleavage products of various DNA substrates showed that Zan I endonuclease is an isoschizomer of Bst NI and Eco RII endonucleases. The conditions for the maximum activity of this enzyme were determined which is different from those of Bst NI and Eco RII endonuclease. 3. DNA protection by Alu I, Hpa II and Hha I Methylases Hexameric restriction endonucleases can be inhibited by the methylation on the internal tetrameric sequences. The degree of inhibitions by Alu I, Hpa II and Hha I methylases allow us to predict the specificities of various hexameric restriction methylases which have never been isolated. On the other hand, the results could be the important informations for the cDNA cloning experiments using restriction linker DNAs.