Literature DB >> 1101972

[Quaternary structure of Escherichia coli polynucleotide phosphorylase: chemical characterization of form A].

C Portier.   

Abstract

We had previously shown the existence of two classes of polynucleotide phosphorylases : Form A which is made of alpha chains and carries the catalytic sites ; and form B which is constituted of alpha chains and of beta chains. We performed some chemical analyses of form A (N-terminal sequence, amino acid composition, peptide mapping) which suggest that the alpha chains are all identical and moreover that they have no relationship with the beta chains. The latter do not therefore derive from a partial proteolytic degradation of the alpha chains and can therefore be considered as true subunits of the enzyme.

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Year:  1975        PMID: 1101972     DOI: 10.1016/s0300-9084(75)80134-9

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  2 in total

1.  Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase.

Authors:  A Guissani; C Portier
Journal:  Nucleic Acids Res       Date:  1976-11       Impact factor: 16.971

2.  Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions.

Authors:  C Portier; P Regnier
Journal:  Nucleic Acids Res       Date:  1984-08-10       Impact factor: 16.971

  2 in total

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