Literature DB >> 6351929

Purification and properties of the antizymes of Escherichia coli to ornithine decarboxylase.

J S Heller, D A Kyriakidis, E S Canellakis.   

Abstract

The purification of the antizymes to ornithine decarboxylase of Escherichia coli to homogeneity is detailed. An acidic component, pI 3.8, and two basic histone-like proteins, pI above 9.5, are described. The two latter proteins constitute approximately 90% of the total antizyme activity.

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Year:  1983        PMID： 6351929     DOI： 10.1016/0304-4165(83)90137-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  4 in total

1.  Characterization of ornithine decarboxylase and regulation by its antizyme in Thermus thermophilus.

Authors:  A A Pantazaki; C G Anagnostopoulos; E E Lioliou; D A Kyriakidis
Journal:  Mol Cell Biochem       Date:  1999-05       Impact factor: 3.396

Review 2.  Polyamines in microorganisms.

Authors:  C W Tabor; H Tabor
Journal:  Microbiol Rev       Date:  1985-03

Review 3.  Rapid and regulated degradation of ornithine decarboxylase.

Authors:  S Hayashi; Y Murakami
Journal:  Biochem J       Date:  1995-02-15       Impact factor: 3.857

4.  Identification, cloning, and nucleotide sequencing of the ornithine decarboxylase antizyme gene of Escherichia coli.

Authors:  E S Canellakis; A A Paterakis; S C Huang; C A Panagiotidis; D A Kyriakidis
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-01       Impact factor: 11.205
  4 in total

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