Cancer Research Annual Meeting 2010  2010 Workshops
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online

[Cancer Research 36, 2216-2222, July 1, 1976]
© 1976 American Association for Cancer Research

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ohashi, M.
Right arrow Articles by Taguchi, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohashi, M.
Right arrow Articles by Taguchi, T.

Two Forms of Thymidine Kinase in Normal and Tumor Tissues of Animals1

Mochihiko Ohashi2 and Takahiko Taguchi

Department of Biochemistry, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173, Japan

2 To whom requests for reprints should be addressed.

The thymidine kinases extracted from the spleen of mice infected with Friend virus and from Yoshida sarcoma in rats were separated into two active peaks by diethylaminoethyl cellulose column chromatography, while those of normal tissues have been found to consist of only the first peak (P-I). The second peak (P-II) was also found in the enzyme from the extract of the spleen when the animals were treated by i.p. injections of 1-acetyl-2-phenylhydrazine. The two P-II peaks from tumor tissue and from spleen enlarged by anemia-inducing agents were indistinguishable on the chromatographic profile. On the other hand, the thymidine kinase extracted with Triton X-100 from a mitochondrial fraction of normal liver was found to consist of only one peak in the same position as the above P-II's on the chromatogram, but its faculty for deoxythymidine triphosphate inhibition was not identical to that of tumor tissue. This treatment with the detergent might cause dissociation of a certain component from the enzyme complex to make the extra peak (P-IIb), but it eventually shifts to P-II on the chromatogram.

1 This work was supported in part by Grant-in-Aid 901010 for Cancer Research from the Ministry of Education, Science and Culture, Japan.

Received 8/ 4/75. Accepted 3/11/76.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1976 by the American Association for Cancer Research.