Literature DB >> 1173055

Poly (A) polymerase of bovine lymphosarcoma.

A A Keshgegian, S M Meltzer, J J Furth.   

Abstract

Poly(A) polymerase has been extensively purified from low-salt extracts of bovine lymphosarcoma. The enzyme is Mn2+ dependent, requires an oligonucleotide or RNA primer, incorporates only adenosine triphosphate, and is inhibited by other ribonucleotides or deoxynucleotides. Oligoadenylate and ribosomal RNA are good primers for the enzyme; transfer RNA and poly(A) are poor. RNA transcribed in vitro by homologous RNA polymerase is an efficient primer. The properties of the enzyme are similar to the properties of the Mn2+ -activated poly(A) polymerase of calf thymus. Approximately the same amount of enzyme appears to be present in lymphosarcoma and calf thymus.

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Year:  1975        PMID: 1173055

Source DB:  PubMed          Journal:  Cancer Res        ISSN: 0008-5472            Impact factor:   12.701


  1 in total

1.  Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain.

Authors:  A Zhelkovsky; S Helmling; C Moore
Journal:  Mol Cell Biol       Date:  1998-10       Impact factor: 4.272

  1 in total

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