Purification and characterization of DNA-relaxing enzyme from Haemophilus gallinarium.
Biochim Biophys Acta
; 563(1): 261-5, 1979 Jun 20.
Article
in En
| MEDLINE
| ID: mdl-227461
ABSTRACT
A DNA-relaxing enzyme capable of concerted nicking and closing of DNA backbone bonds has been purified from Haemophilus gallinarum by two chromatographic steps and gel filtration. The enzyme efficiently catalyzes the removal of superhelical turns from a negatively twisted DNA and requires Mg2+ for this activity. Slight removal of superhelical turns from a positively twisted DNA generated by binding of ethidium bromide is found, but only at high enzyme concentrations. The DNA-relaxing activity is inhibited markedly with heat-denatured DNA, whereas native DNA and RNA have almost no affect on this activity.
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Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Haemophilus
/
DNA Topoisomerases, Type I
Language:
En
Journal:
Biochim Biophys Acta
Year:
1979
Type:
Article