DNA topoisomerase from Agrobacterium tumefaciens: purification and catalytic properties.

Abstract:

:The DNA topoisomerase from Agrobacterium tumefaciens has been purified to apparent homogeneity. The enzyme is a single polypeptide of about 100,000 in molecular weight. No apparent separation of the nicking and sealing activities could be obtained in attempts to separate the two activities by a variety of methods, including limited protease digestion, thermal denaturation, and differential inhibition. Monoclonal antibodies obtained from hybridomas likewise did not preferentially inhibit one of the two activities. These results suggest that the two catalytic functions are carried by the same essential residues of the active enzyme site.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

LeBon JM,Agarwal S,Chirikjian JG

doi

10.1093/nar/9.4.909

subject

Has Abstract

pub_date

1981-02-25 00:00:00

pages

909-20

issue

4

eissn

0305-1048

issn

1362-4962

journal_volume

9

pub_type

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