DNA primase activity found in an alpha-like DNA polymerase obtained from Halobacterium halobium.

Abstract:

An aphidicolin-sensitive DNA polymerase was purified from extracts of Halobacterium halobium. The analysis of this alpha-like DNA polymerase on polyacrylamide gels under denaturing conditions revealed two peptides with molecular masses of 70 kDa and 60 kDa in equal amounts. Like the DNA polymerase alpha isolated from eukaryotes, the alpha-like DNA polymerase possesses primase activity using UTP and polydeoxyadenylate as template. The primase activity was sensitive to aphidicolin and inhibited by an antiserum against the alpha-like DNA polymerase of H. halobium. The primase activity was dependent on the presence of high salt concentrations.

Polymerases:

Topics:

Status:

new topics/pols set partial results complete validated

Results:

No results available for this paper.

Entry validated by:

Log in to edit reference All References

Using Polbase tables:

Sorting:

Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

Filtering:

It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.