Characterization of human DNA polymerase delta and its immunochemical relationships with DNA polymerase alpha and epsilon.

Abstract:

DNA polymerase delta was purified from human placenta and its polymerase catalytic subunit identified as a 125-kDa polypeptide by activity staining. This 125-kDa form of DNA polymerase delta resembles that reported from calf thymus (Lee, M. Y. W. T., Tan, C.-K., Downey, K. M., and So, A. G. (1984) Biochemistry 23, 1906-1913) and differs in molecular properties from a previously described form isolated from human placenta (Lee, M. Y. W. T., and Toomey, N. L. (1987) Biochemistry 26, 1076-1085) and now referred to as DNA polymerase epsilon. The properties of DNA polymerase delta were further investigated to determine its relationships with DNA polymerase epsilon. The two enzymes differed in their response to proliferating cell nuclear antigen. Monoclonal antibodies against DNA polymerase delta were raised and used to examine its immunochemical relationships with DNA polymerase alpha and epsilon. These studies provided evidence that all three proteins are structurally distinct but share a common epitope(s). Immunofluorescence microscopy indicates that DNA polymerase delta and possibly also DNA polymerase epsilon are localized to the nucleus.

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.