Purification and characterization of deoxyribonuclease from small intestine of camel Camelus dromedarius
Somia S. Abdel-Gany | Mohamed O. El-Badry | Afaf S. Fahmy | Saleh A. Mohamed
The chromatography of deoxyribonuclease (DNase) from small intestine of camel Camelus dromedarius by DEAE-Sepharose separated three isoforms DNase 1, DNase 2 and DNase 3. The DNase 3 was purified to homogeneity by chromatography on Sephacryl S-200. The molecular weight of DNase 3 was 30 kDa using gel filtration and SDS-PAGE. The pH optimum of DNase 3 was reported at 7.0 using Tris-HCl buffer. The temperature optimum of DNase 3 was found to be 50 °C. The enzyme was stable up to 50 °C for one h incubation. The Km value was 28.5 µg DNA, where this low value indicated the high affinity of enzyme toward DNA as substrate. No activity of DNase 3 was determined in the absence of metal cations. Mg2+ and Ca2+ caused significant enhancement in the enzyme activity by 90 and 75%, respectively. The mixture of Mg2+ and Ca2+ caused 100% of enzyme activity. Ni2+, Co2+, Ba2+, Zn2+ and Cd2+ showed very strong inhibitory effect on enzyme activity. In conclusion, the characterization of DNase 3 indicated that the enzyme is considered as a member of DNase I family. The low Km value of the DNA suggested that the high digestion of DNA of camel forage by small intestine DNase 3.
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