Skip Navigation

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 Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hirasawa, E.
Right arrow Articles by Matsumoto, H.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Hirasawa, E.
Right arrow Articles by Matsumoto, H.
Agricola
Right arrow Articles by Hirasawa, E.
Right arrow Articles by Matsumoto, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1982, Vol. 23, No. 3 417-425
© 1982

Article

Distribution and Properties of Chromatin-Associated Nucleoside Triphosphate Diphosphatase Purified by a New Method

Eiji Hirasawa1 and Hideaki Matsumoto2

1Department of Biology, Faculty of Science, Osaka City University Sumiyoshi-ku, Osaka 558, Japan
2Institute for Agricultural and Biological Sciences, Okayama University Chuo 2-20-1, Kurashiki, Okayama 710, Japan

Chromatin-associated nucleoside triphosphate diphosphatase (NTDPase) activity was detected in Alaska pea plant only at the germination stage in a study of the plant's development over 5 month from the dormant to fruiting stages. This enzyme activity was also detected in seedlings of several dicotyledonous plants including soybean, Usui pea, cowpea and cucumber, but almost none was found in monocotyledonous corn and rice plants.

When the chromatin of pea epicotyl was fractionated into template-active and -inactive forms by DNase II digestion, most of the NTDPase activity was found in the active chromatin.

A new method to rapidly isolate and purify NTDPase from pea epicotyl chromatin was developed in which NTDPase was eluted with a linear gradient of NaCl on a column packed with cellulose powder and chromatin. DNA remained on the column and the eluted NTDPase was purified further by chromatography using trimethylamino-2-hydroxypropyl cellulose (TMAP-cellulose) and a Sephadex G-100 column, which give chromatin 18-fold purer than the starting sample.

This purified NTDPase was adsorbed by DNA-cellulose, which is further evidence that NTDPase is a kind of non-histone protein associated with DNA. Several cations including Ca2$, Mg2$, Mn2$ and Zn2$ stimulated the enzyme activity, with the maximal eightfold activation by Ca2$. NTDPase activity was clearly inhibited by KCN and pyrophosphate, but not by SH-blocking inhibitors and various metal chelators at 1 mM.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.