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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
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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.

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