Purification of an acidic deoxyribonuclease II from the primate spleen

@article{Pitout1974PurificationOA,
  title={Purification of an acidic deoxyribonuclease II from the primate spleen},
  author={Marthinus Pitout and P. G. Kempff and Johannes C. Schabort},
  journal={International Journal of Biochemistry},
  year={1974},
  volume={5},
  pages={241-246}
}
6 Citations
Mechanism of action of deoxyribonuclease II from human lymphoblasts.
TLDR
Application of DNA sequencing techniques has further revealed a unique resistance of 3' termini to hydrolysis by this enzyme, and the presence of 3'-phosphoryl termini on the DNA cleavage products was confirmed since they failed to function as primers for DNA synthesis catalyzed by Escherichia coli DNA polymerase I.
Mammalian nucleolytic enzymes.
DNase II in bull and ram sperm tail and mitochondria.
TLDR
Extracts of bull and ram sperm tails prepared by DTT and CTAB treatment contained deoxyribonuclease II, degrading only native double-stranded DNA at acid pH (3.9--4.5).

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The results obtained strongly indicate that the enzymatic activity is associated with protein molecules endowed with very similar physical, chemical, and enzymic properties.
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