Skip Navigation

This Article
Right arrow Print PDF (1379K)
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (35)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Klimczak, L.
Right arrow Articles by Burger, K. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klimczak, L.
Right arrow Articles by Burger, K. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1985, Vol. 13, No. 14 5269-5282
© 1985

Articles

Purification and characterization of DNA polymerase from the archaebacterium Sulfolobus acidocaldarius

Leszek Klimczak*, Friedrich Grummt+ and Klaus J. Burger

Institut für Genetik und Mikrobiologie Röntgenring 11 D-8700 Würzburg, FRG +Institut für Biochemie, Universität Würzburg Röntgenring 11 D-8700 Würzburg, FRG

*To whom correspondence should be addressed

Received May 16, 1985. Accepted June 20, 1985.

DNA polymerase has been purified about 25,000-fold from the thermoacidophilic archaebacterium Sulfolobus acidocaldarjus. On SDS-PAGE the enzyme was observed to have a molecular weight of 100 kDa and to be about 90% pure. The native molecular weight was 108 kDa indicating that the enzyme is composed of a single polypeptide. Activity gel analysis showed an active polypeptide of about 100 kDa. under conditions promoting proteolysis this polypeptide was degraded to a slightly smaller form of 98 kDa. The enzyme has been characterized in respect to optimal assay conditions, template specificity, sensitivity to inhibitors and associated nuclease activities. The high temperature optimum of 65°C should be emphasized. No substantial similarities have been found with other prokaryotic and eukaryotic DNA polymerases, although the enzyme bears certain resemblances to prokaryotic non-replicative polymerases.


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


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
I. K. O. Cann, S. Ishino, N. Nomura, Y. Sako, and Y. Ishino
Two Family B DNA Polymerases from Aeropyrum pernix, an Aerobic Hyperthermophilic Crenarchaeote
J. Bacteriol., October 1, 1999; 181(19): 5984 - 5992.
[Abstract] [Full Text]

Home page
 GeneticsHome page
I. K. O. Cann and Y. Ishino
Archaeal DNA Replication: Identifying the Pieces to Solve a Puzzle
Genetics, August 1, 1999; 152(4): 1249 - 1267.
[Abstract] [Full Text]

Home page
 Genome ResHome page
F C Lawyer, S Stoffel, R K Saiki, S Y Chang, P A Landre, R D Abramson, and D H Gelfand
High-level expression, purification, and enzymatic characterization of full-length Thermus aquaticus DNA polymerase and a truncated form deficient in 5' to 3' exonuclease activity.
Genome Res., May 1, 1993; 2(4): 275 - 287.
[Abstract] [PDF]


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.