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Casein Kinase Ⅱ에 의한 송아지 흉선 DNA Topoisomerase Ⅱ 의 활성조절
이경희,배영석 ( Kyung Hee Lee,Young Seuk Bae ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.2
In order to study the modulation mechanism of topoisomerase II (topo II) activity, casein kinase II was purified from bovine liver using DEAF-cellulose, phosphocellulose, hydroxyapatite, and heparin-agarose column chromatography. Analysis of the purified enzyme by sodium dodesyl sulfate-polyacrylamide gel electrophoresis revealed three bands of molecular mass of 44, 42, and 26 kDa. Casein kinase II phosphorylated calf thymus topo II, and the phosphorylation stimulated topo II activity by 2 fold over that of unmodified enzyme. The treatment of calf thymus topo II with alkaline phosphatase abolished the enzyme activity almost completely. These results suggest that some of topo II enzymes exist as phosphoproteins in calf thymus and calf thymus topo II activity can be regulated by casein kinase II.
소의 DNA topoisomerase 2 에 의한 비상동적 재조합 1. DNA 재조합 연구를 위한 모델 system 의 개발
김현숙,이경희,박진우,배영석,문병조 경북대학교 유전공학연구소 1992 遺傳工學硏究所報 Vol.7 No.1
In order to investigate potential roles for topoisomerase II (topo II)-mediated DNA recombination, we have developed in vitro system. DNA topo II has been purified from calf thymus nuclei by using P4 phage knotted DNA as substrate The purified enzyme consists of two bands of apparent molecular masses of 170 and 160kd, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and Mg^(2+) and free of any nucleolytic, proteolytic or topoisomerase I (topo I) activity. In addition, for substrate DNA of recombination reaction we have constructed shuttle vectors, which contain two bacterial markers, amp and neo, the replication origins of pBR322 and SV40 DNA, and topo II consensus sequence.