@article{oai:teapot.lib.ocha.ac.jp:00034694,
 author = {Ikeda, Fumi and Matsumoto, Yoshihisa and Suzuki, Norio and Murakami-Murofushi, Kimiko},
 issue = {1},
 journal = {お茶の水女子大學自然科學報告},
 month = {Aug},
 note = {application/pdf, 紀要論文, Telomerase is known as a ribonucleoprotein enzyme essential for the repair of replication-induced deletion of chromosome terminal in most eukaryotes. Although the regulatory mechanism of telomerase inactivation and re-activation has not yet been clarified, there is a possibility that telomerase activity is regulated by phosphorylation and dephosphorylation. DNA-dependent protein kinase (DNA-PK) is considered to be a critical enzyme in DNA double-strand break repair and possibility of involvement of this enzyme in the regulation of telomerase is expected. To examin correlation between telomerase and DNA-PK, we purified DNA-PK from human leukaemic MOLT-4 cells by successive column chromatography. Through the conventional process of purification, DNA-PK activity was accompanied by telomerase activity. We used modified purification protcol in this study, and tinaly, succeeded in purification of DNA-PK separately from telomerase activity. This DNA-PK didn't show any effect on the telomerase activity, and these results indicate that the telomerase may not be regulated via phosphorylation with DNA-PK.},
 pages = {7--12},
 title = {Examination of The Correlation between DNA-dependent Protein Kinase and Telomerase Activity},
 volume = {49},
 year = {1998}
}