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Nucleic Acids Research, 1984, Vol. 12, No. 3 1391-1400
© 1984

ENZYMOLOGY

Chromatin prepared using micrococcal nuclease retains the enzyme activity which can be removed with cation-exchange resin AG 50 WX2

Shakuntla B. Goel and Sohan P. Modak

Department of Zoology, University of Poona Pune 411007, India

To whom the reprint-requests may be addressed

Received November 30, 1983. Accepted January 3, 1984.

Micrococcal nuclease used to digest nuclei remains bound to the chromatin in an inactive form. The enzyme activity can be restored in situ by addition of divalent cations such as Ca++ or Mg++ resulting in continued digestion of high molecular weight chromatin into smaller fragments as demonstrated by two dimensional gel electrophoresis of samples as chromatin and DNA in the first and second dimensions, respectively. The bound enzyme can be selectively removed from the chromatin by treatment with cation exchange resin AG 50 WX2 at low salt concentration without altering the electrophoretic mobility of the chromatin.

This work represents a partial fulfillment of the Ph.D. thesis of S.B.G.


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