Literature DB >> 241642

Co-fractionation of an endonuclease activity during the purification of DNA polymerase-alpha from regenerating rat liver. Properties and separation from DNA polymerase.

M Mechali, A M de Recondo.   

Abstract

The presence of endonuclease activity associated with DNA polymerase was detected during the purification of high-molecular-weight DNA polymerase-alpha from regenerating rat liver by the use of a highly sensitive test. This endonuclease activity co-fractionated with DNA polymerase in a great variety of purification procedures involving ion-exchange chromatographies or molecular weight fractionation, but was further completely separated from DNA polymerase activity by using affinity chromatography on DNA-cellulose. The endonuclease acted on native or denatured DNA by introducing single-strand nicks in the DNA molecules; its enzymatic properties indicate that it could act in polymerisation conditions in vitro.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 241642     DOI: 10.1111/j.1432-1033.1975.tb02393.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  HeLa DNA polymerase alpha activity in vitro: specific stimulation by a non-enzymic protein factor.

Authors:  B Novak; E F Baril
Journal:  Nucleic Acids Res       Date:  1978-01       Impact factor: 16.971

2.  DNA polymerase activities in growing cells infected with simian virus 40.

Authors:  M Méchali; M Girard; A M de Recondo
Journal:  J Virol       Date:  1977-07       Impact factor: 5.103

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.