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. 1989 Jun 12;17(11):4047–4060. doi: 10.1093/nar/17.11.4047

Characterization of a novel endonuclease from Crithidia fasciculata.

M L Holdsworth 1, J C Hines 1, D S Ray 1
PMCID: PMC317918  PMID: 2544854

Abstract

A new endonuclease activity has been identified in whole cell lysates of the trypanosomatid Crithidia fasciculata. This activity, termed endonuclease A (Endo A), introduces single-strand breaks at highly preferred sites in double stranded DNA substrates Physical analysis of this enzyme indicates that it has a sedimentation coefficient S20,W of 4.9 and a Stokes radius of 59A and thus, a native molecular weight of 125,000 and a frictional coefficient of 1.8. A monomeric structure is suggested for the enzyme based on the recovery of Endo A activity associated with a polypeptide with a molecular weight of 116,000-120,000, following electrophoresis on sodium dodecyl sulfate polyacrylamide gels. Endo A shows an absolute requirement for Mg2+ or Mn2+ and exhibits activity over a broad pH and temperature range, with optimal conditions for activity at pH 8.0 and 30 degrees C.

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Selected References

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