Structure of DNA polymerase alpha-primase complexes from mammalian cells analyzed by using monoclonal antibodies.

Abstract:

:The molecular masses of two of the four DNA polymerase alpha-primase complex subunit peptides from various mammalian cells have been compared through the use of specific monoclonal antibodies. One monoclonal antibody (E4) binds to 77-kDa peptide from HeLa cells and cognate peptides from other mammalian cells (monkey, mouse, bovine, Indian muntjac, and hamster). Another monoclonal antibody (A5) binds the 180-kDa type peptide and its degradation product (160-kDa peptide) of the mammalian DNA polymerase alpha-primase complexes. Neither of these antibodies reacts with DNA polymerase alpha-primase complex from chicken cells. Comparative immunoblot analysis indicates that the molecular masses of the two main peptides of DNA polymerase alpha-primase complex isolated from the various mammalian sources are in excellent agreement with each other, except for the 77-kDa type peptide from bovine and Indian muntjac cells which was found to be significantly smaller (68 kDa) in these cases. The small molecular mass of bovine 77-kDa type peptide is not attributable to the action of a protease which may be present in the extract of bovine cells.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kozu T,Nikaido K,Yagura T

doi

10.1093/oxfordjournals.jbchem.a123081

subject

Has Abstract

pub_date

1990-04-01 00:00:00

pages

535-8

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

107

pub_type

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