Purification and characterization of Xenopus laevis topoisomerase II.
AUTOR(ES)
Benedetti, P
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555276Documentos Relacionados
- Isolation and characterization of the gene encoding Drosophila DNA topoisomerase II.
- Cloning and characterization of the gene for the somatic form of DNA topoisomerase I from Xenopus laevis.
- Purification, immunological and biochemical characterization of Ap4A binding protein from Xenopus laevis oocytes.
- Purification and characterization of Escherichia coli heat-stable enterotoxin II.
- Fine structure of ribosomal RNA. II. Distribution of methylated sequences within Xenopus laevis rRNA.