Literature DB >> 1009968

An endonuclease from mouse cells specific for single-stranded DNA.

B Otto, R Knippers.   

Abstract

An endonuclease with a molecular weight of about 70000 (5-6S) was extensively purified from mouse ascites cells. The enzyme specifically attacks single-stranded DNA which is degraded mainly to oligonucleotides, with 5-10 residues. Supercoiled covalently closed circular phage DNA is converted to the linear relaxed form. The enzyme activity is highly sensitive to salt and can be stimulated by reagents lowering the dielectric constant of the buffer such as dimethylsulfoxide and glycerol.

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Year:  1976        PMID: 1009968     DOI: 10.1111/j.1432-1033.1976.tb11153.x

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


  3 in total

1.  Adenovirus-induced inhibition of cellular DNase.

Authors:  K Nass; G D Frenkel
Journal:  J Virol       Date:  1978-05       Impact factor: 5.103

2.  Binding of phosphorylated histone H1 to DNA.

Authors:  R Knippers; B Otto; R Böhme
Journal:  Nucleic Acids Res       Date:  1978-06       Impact factor: 16.971

3.  Purification and properties of a single strand-specific endonuclease from mouse cell mitochondria.

Authors:  A E Tomkinson; S Linn
Journal:  Nucleic Acids Res       Date:  1986-12-22       Impact factor: 16.971

  3 in total

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