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Monoclonal antibody that blocks phosphoinositide-dependent activation of mouse tumor DNA polymerase alpha.

Abstract：

:A monoclonal antibody (MaB) against mouse sarcoma DNA polymerase alpha was isolated from the culture medium of an IgG-secreting hybridoma. The MaB demonstrated reactivity against two murine DNA polymerase alpha preparations and a calf thymus DNA polymerase alpha. Murine sarcoma polymerase was activated in vitro by phosphatidylinositol-4-monophosphate (PIP) showing increased deoxynucleotidyltransferase activity and enhanced binding affinity to activated DNA template. The MaB did not neutralize polymerase activity, but blocked further activation of the enzyme by PIP. Treatment of polymerase with MaB prior to treatment with PIP inhibited both increased enzyme activation and increased binding of the enzyme to DNA template. Treatment of polymerase with MaB subsequent to treatment with PIP did not block enzyme activation or increased DNA template binding. The data suggest that this anti-DNA polymerase alpha IgG is directed against a regulatory subunit of the polymerase rather than the catalytic subunit. The antibody may serve to distinguish between DNA polymerase alpha preparations with distinctly different regulatory subunits.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sylvia VL,Norman JO,Curtin GM,Busbee DL

doi

10.1016/s0006-291x(86)80334-5

subject

Has Abstract

pub_date

1986-11-26 00:00:00

pages

60-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(86)80334-5

journal_volume

141

pub_type

杂志文章

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