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Ruminant Nutrition and Forage Utilization
Asian-Australasian Journal of Animal Sciences 1990;3(2): 115-120.
DOI: https://doi.org/10.5713/ajas.1990.115    Published online June 1, 1990.
Purification and properities of extracellular nuclease(s) from rumen contents of Bubalus Bubalis
P. R. Sinha, S. M. Dutta
Extracellular nuclease(s) in buffalo rumen fluid were purified from strained rumen fluid by a procedure involving Seitz filtration, acetone fractionation and gel filtration on Sephadex G-100. The enzyme corresponding to peaks I and II were approximately 30,000 and 12,000 respectively. The properties of enzymes from the two peaks, however, were same. Optimum temperature for both DNase and RNase activities was at 50째C. Whereas DNase activity was stable upto 60째C, RNase activity was stable only upto 50째C. DNase activity recorded two pH optima, one at pH 5.5 and the other at pH 7.0. RNase activity recorded a broad pH optimum between pH 6.0-8.0. pH stability of the enzyme coincided with pH optima for both the activities. DNase activity was stimulated by Mg2+ and Mn2+ and inhibited by Fe2+, Zn2+, Hg2+ and Ag+. RNase activity was also stimulated by Mg2+ and Mn2+ and inhibited by Cu2+, Fe2+, Zn2+, Hg2+ and Ag+. Reducing agents stimulated both the activities.
Keywords: Ribonuclease; Deoxyribonuclease; Rumen; Buffalo

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