English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38102
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Characterization of a 3'->5' exonuclease activity in the phage ø29-encoded DNA polymerase

AuthorsBlanco, Luis ; Salas, Margarita
Issue Date1985
PublisherOxford University Press
CitationNucleic Acids Research 13(4): 1239-1249 (1985)
AbstractPurified protein p2 of phage φ29, characterized as a specific DNA polymerase involved in the initiation and elongation of φ29 DNA replication, contains a 3′ → 5′ exonuclease active on single-stranded DNA, but not on double-stranded DNA. No 5′→3′ exonuclease activity was found. The 3′→5′ exonuclease activity was shown to be associated with the DNA polymerase since 1) the two activities were heat-inactivated with identical kinetics and 2) both activities, present in purified protein p2, cosedimented in a glycerol gradient.
Publisher version (URL)http://dx.doi.org/10.1093/nar/13.4.1239
Appears in Collections:(CBM) Artículos
Files in This Item:
File Description SizeFormat 
referencia93.pdf1,09 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.