A type 1 DNA topoisomerase from the kinetoplast hemoflagellate Leishmania donovani.
Indian J Biochem Biophys
;
1993 Oct; 30(5): 257-63
Article
in English
| IMSEAR
| ID: sea-27867
ABSTRACT
A type 1 DNA topoisomerase has been purified from the nuclei of the kinetoplast hemoflagellate Leishmania donovani using polyethylene glycol fractionation and chromatography on hydroxylapatite, phosphocellulose and phenylsepharose column. The relaxation activity is ATP independent. Mg2+ is an essential cofactor for the reaction with an optimum at 10 mM. Mg2+ can be substituted by Mn2+ at 5 mM concentration. The relaxation reaction exhibits a salt optimum at 100 mM KCl. The enzyme can not remove supercoils from positive superhelical DNAs nor can induce supercoiling of relaxed DNAs. The topoisomerase activity is associated with a polypeptide of molecular weight about 67 kDa as shown by sephacryl-S200 gel filtration and by electrophoresis on sodium dodecyl sulphate-polyacrylamide gels.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Polyethylene Glycols
/
Leishmania donovani
/
Kinetics
/
Cell Nucleus
/
Chromatography
/
Chromatography, Ion Exchange
/
Durapatite
/
DNA, Kinetoplast
/
DNA Topoisomerases, Type I
/
Animals
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1993
Type:
Article
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