Purification and characterization of mouse DNA polymerase alpha devoid of primase activity.

Abstract:

:A simple method was developed for the isolation of primase-free DNA polymerase-alpha from the DNA polymerase-alpha-primase complex of mouse FM3A cells. The polymerase was separated from primase subunits by chromatography on a single-stranded DNA-cellulose column in the presence of 50% etylene glycol. The primase-free DNA polymerase-alpha contained two polypeptides with molecular masses of 180,000 and 68,000. Analysis of the DNA products with poly(dA)-oligo(dT)10 as template-primer revealed that both primase-free DNA polymerase-alpha and the DNA polymerase-alpha-primase complex predominantly synthesized short DNA with less than 30 nucleotides, but that the DNA polymerase-alpha-primase complex also synthesized some longer DNA with more than 300-400 nucleotides.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Takada-Takayama R,Suzuki M,Enomoto T,Hanaoka F,Ui M

doi

10.1016/0014-5793(90)81043-n

subject

Has Abstract

pub_date

1990-10-29 00:00:00

pages

27-30

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)81043-N

journal_volume

273

pub_type

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