Literature DB >> 485149

Purification of an Endogenous polynucleotide phosphorylase from Brevibacterium JM98A.

H H Yang, D W Thayer, S P Yang.   

Abstract

Polynucleotide phosphorylase was purified form Brevibacterium JM98A (ATCC 29895). Homopolynucleotides were arsenolysed in the order polyadenylate greater than polycytidylic acid greater than polyuridylic acid greater than polyguanylate. The products were ribonucleoside 5'-monophosphates.

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Year:  1979        PMID： 485149      PMCID： PMC243450          DOI： 10.1128/aem.38.1.159-161.1979

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN： 0099-2240            Impact factor:   4.792


  3 in total

1.  Polynucleotide phosphorylase of Micrococcus lysodeikticus. II. Further purification of the enzyme and the arsenolysis of polyribonucleotides.

Authors:  M F SINGER; B M O'BRIEN
Journal:  J Biol Chem       Date:  1963-01       Impact factor: 5.157

2.  Thermostable polynucleotide phosphorylases from Bacillus stearothermophilus and Thermus aquaticus.

Authors:  J N Wood; D W Hutchinson
Journal:  Nucleic Acids Res       Date:  1976-01       Impact factor: 16.971

3.  Reduction of endogenous nucleic acid in a single-cell protein.

Authors:  H H Yang; D W Thayer; S P Yang
Journal:  Appl Environ Microbiol       Date:  1979-07       Impact factor: 4.792
  3 in total

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