English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Characterisation of size variants of type I DNA topoisomerase isolated from calf thymus

Schmitt, B., Schuh-Buhre, U., & Vosberg, H.-P. (1984). Characterisation of size variants of type I DNA topoisomerase isolated from calf thymus. European Journal of Biochemistry, 144(1), 127-134. doi:10.1111/j.1432-1033.1984.tb08440.x.

Item is

Files

show Files
hide Files
:
EurJBiochem_144_1984_127.pdf (Any fulltext), 936KB
 
File Permalink:
-
Name:
EurJBiochem_144_1984_127.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Schmitt, Bertram1, Author           
Schuh-Buhre, Ursula2, Author           
Vosberg, Hans-Peter3, Author           
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              
3Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

Content

show
hide
Free keywords: -
 Abstract: Calf thymus DNA topoisomerase I, which belongs to the eukaryotic type I topoisomerases, is in a typical preparation purified as a set of five major polypeptides with Mr between 70000 and 100000. At least four of these proteins have binding affinity for DNA as was shown by incubating them with radioactive single-stranded DNA after separation in dodecylsulfate polyacrylamide gels and blotting onto nitrocellulose filters. That these polypeptides have DNA relaxing activity was directly demonstrated with protein extracted from single bands of dodecylsulfate/polyacrylamide gels. We consider the 100000-Mr protein to be the native enzyme. The smaller components are catalytically active fragments of the native topoisomerase most probably arising from limited proteolysis either within the nucleus or during the purification of the enzyme. In two-dimensional non-equilibrium pH-gradient electrophoresis gels the topoisomerase size variants exhibit apparent pI values between 8.1 and 8.3, with small but distinct differences between the components. The calf thymus topoisomerase I, upon binding to phage fd-DNA, protects a stretch of 15-25 nucleotides against digestion with DNase I.

Details

show
hide
Language(s): eng - English
 Dates: 1984-04-091984-06-252005-03-031984-10
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: European Journal of Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 144 (1) Sequence Number: - Start / End Page: 127 - 134 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040