Literature DB >> 15625871

Particulate DNA polymerase from the cytoplasm of Xenopus laevis oocytes.

M I Baldi1, P Bazzicalupo, G P Tocchini-Valentini.   

Abstract

A DNA polymerase has been partially purified and characterized from Xenopus laevis stage 6 oocytes. The enzyme is present only in the cytoplasm and has been shown to be able to copy Poly(A) x oligo(dT), to be sensitive to N-ethylmaleimide, and to sediment faster than 4 S in high salt glycerol gradient. The enzyme can be extracted from particulate material which has a density in sucrose gradient ranging from 1.200 to 1.225 g/cc. This particulate material is identified by its ability to use Poly(A) x oligo(dT) as template in an exogenous DNA polymerase reaction and by its endogenous DNA synthesizing capacity.

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Year:  1976        PMID: 15625871     DOI: 10.1016/0006-291x(76)90219-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Purification of a DNA-binding protein from Xenopus laevis unfertilized eggs.

Authors:  G Carrara; S Gattoni; D Mercanti; G P Tocchini-Valentini
Journal:  Nucleic Acids Res       Date:  1977-08       Impact factor: 16.971

  1 in total

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