Premium
Purification and characterization of Xenopus laevis topoisomerase II.
Author(s) -
Benedetti P.,
Baldi M.I.,
Mattoccia E.,
TocchiniValentini G.P.
Publication year - 1983
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1983.tb01585.x
Subject(s) - biology , xenopus , topoisomerase , computational biology , salientia , microbiology and biotechnology , genetics , dna , gene
We have purified to apparent homogeneity a type II DNA topoisomerase from Xenopus laevis oocyte nuclei (germinal vesicles, or GV). The most pure preparations contain a single polypeptide of 175,000 daltons as determined by SDS‐gel electrophoresis. The enzyme changes the linking number of DNA circles in steps of two and reversibly knots or catenates DNA rings. No gyrase activity is detectable and ATP is required.