Go to Top Go to Bottom
Ruminant Nutrition and Forage Utilization
Asian-Australasian Journal of Animal Sciences 1990;3(2): 115-120.
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
Abstract
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
TOOLS
METRICS Graph View
  • 0 Crossref
  •  0 Scopus
  • 2,827 View
  • 15 Download
Related articles

Purification and Properties of Bovine Skeletal Muscle Proteasome2005 June;18(6)



Editorial Office
Asian-Australasian Association of Animal Production Societies(AAAP)
Room 708 Sammo Sporex, 23, Sillim-ro 59-gil, Gwanak-gu, Seoul 08776, Korea   
TEL : +82-2-888-6558    FAX : +82-2-888-6559   
E-mail : editor@animbiosci.org               

Copyright © 2024 by Asian-Australasian Association of Animal Production Societies.

Developed in M2PI

Close layer
prev next