Purification and properties of a magnesium-dependent endodeoxyribonuclease endogenous to rat-liver nuclei
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, ISSN: 0167-4781, Vol: 950, Issue: 3, Page: 313-320
1988
- 16Citations
- 1Captures
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Metrics Details
- Citations16
- Citation Indexes16
- 16
- CrossRef7
- Captures1
- Readers1
Article Description
An Mg 2+ -dependent endonuclease has been purified from a 0.6 M NaCl extract of rat-liver nuclei by a series of chromatographic procedures and finally by isoelectric focusing (IEF) electrophoresis. The nuclease fraction prepared by the IEF electrophoresis (IEF fraction) was shown to have a p I value of 7.1 and to migrate as a single band to a molecular-weight position of 36500 on SDS-polyacrylamide gel. The IEF fraction was subjected to a sedimentation analysis. In a hypotonic buffer (10 mM Tris), the nuclease activity sedimented to have an S value of 4.1 S. However, in an isotonic buffer (0.15 M NaCl), this fraction exhibited two activity peaks of 2.8 and 4.3 S. In a hypertonic buffer (0.3 M NaCl), almost all of the nuclease activity sedimented at 2.7–2.8 S. In this connection, values of 2.8 and 4.3 S were determined to correspond to molecular weights of about 36000 and 70000, respectively. Thus, an Mg 2+ -dependent endonuclease, endogenous to rat-liver nuclei, has been inferred to exist in the reversible form of a monomer/homodimer as its native state. Moreover, the IEF fraction formed single-strand nicks more rapidly than double-strand cuts in pBR322 DNA, and preferentially produced deoxyguanosine 5′-monophosphate termini in the DNA at an early incubation time. In addition, RNAase activity was not detected in this fraction.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0167478188901273; http://dx.doi.org/10.1016/0167-4781(88)90127-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0023719582&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/3167056; https://linkinghub.elsevier.com/retrieve/pii/0167478188901273; http://dx.doi.org/10.1016/0167-4781%2888%2990127-3; https://dx.doi.org/10.1016/0167-4781%2888%2990127-3
Elsevier BV
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