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KMID : 0377619720230020225
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Korean Jungang Medical Journal
1972 Volume.23 No. 2 p.225 ~ p.231
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Properties of Membrane-bound Deoxyribonuclease from Rabbit Reticulocytes
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Abstract
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Evidence is presented indicating that deoxyribonuclease(DNase) and ribonuclease (RNase) associated with rabbit reticulocyte membrane are distinct enzyme entities.
The membrane-bound deoxyribonuclease of rabbit reticulocytes was differentiated from reticulocyte membrane-bound ribon uclease(RNase) by Sephadex-G-200 chromatography. The enzyme shows optimal pH around 5 and is more heat-labile than the RNase, being inactivatedd at more than 70´. Mg and Mn ions inhibited the enzyme at 10 mM and 5 mM, respectively, suggesting that the enzyme activity is not dependent on divalent cations.
The enzyme acted on both native, and heat-denatured DNA with preference for the former.
From the studies on product chain length and relationship between enzyme activity and reaction time, it was suggested that the enzyme is endonuclease, not to be associated with exonuclease, and belongs to DNase-II of Lindahl´s classification.
Some protein nature inhibitors were suggested to be present in normal erythrocytes and reticulocytes.
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