Literature DB >> 14826

Characterization of the pH 4.0 endonuclease from adenovirus-type-2-infected KB cells.

U Reif, U Winterhoff, W Doerfler.   

Abstract

The properties of the pH 4.0 endonuclease from adenovirus-type-2-infected KB cells were determined. The enzyme has a molecular weight of approximately 40000. Its pH optimum is at pH 4.0, it is not inhibited by ethylenediaminetetraacetate (EDTA), and it is active at temperatures up to 60 degree C. The enzyme cleaves adenovirus DNA in a stepwise manner. The limit digestion product has a molecular weight of 120000-200000. There is evidence that the cleavage reaction proceeds via an initial single-strand nick. Under the conditions tested the endonuclease did not seem to reveal a high degree of specificity as to the recognition of cleavage sites, or else the sites recognized occurred very frequently.

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Year:  1977        PMID: 14826     DOI: 10.1111/j.1432-1033.1977.tb11322.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Adenovirus early function required for protection of viral and cellular DNA.

Authors:  J C D'Halluin; C Allart; C Cousin; P A Boulanger; G R Martin
Journal:  J Virol       Date:  1979-10       Impact factor: 5.103

2.  Purification and properties of a new DNase activity from KB cells.

Authors:  G D Frenkel; K Randles; N Berns
Journal:  Nucleic Acids Res       Date:  1981-12-11       Impact factor: 16.971

3.  Specificity and mode of cleavage of the pH 4.0 endonuclease from adenovirus type 2 - infected KB cells.

Authors:  R Padmanabhan; S Stabel; U Winterhoff; W Doerfler
Journal:  Nucleic Acids Res       Date:  1979-07-11       Impact factor: 16.971

  3 in total

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