Cytidine deaminase (EC 3.5.4.5) has been partially purified from protoscoleces of Echinococcus granulosus by gel filteration chromatography using Sephadex G200 .The molecular weight of the enzyme determined by gel filteration was about 82000 dalton with specific activity of 826 nmol/min/mg protein and with purification fold of about 27 times . The optimum pH was found to be 7.5 at 37 oC with km value of 0.03 mM for cytidine . The results indicate that the activity of cytidine deaminase was found to be inhibited by 5_flourouracil , 5_thiouracil and allopurinol with inhibitory percentage of 24 % ,18 % and
20%respectively.
F. Hassan,H and A.Saber,J . (2015). Partial purification of cytidine deaminase from protoscoleces of Echinococcus granulosus. Kirkuk Journal of Science, 10(4), 119-133. doi: 10.32894/kujss.2015.124092
MLA
F. Hassan,H , and A.Saber,J . "Partial purification of cytidine deaminase from protoscoleces of Echinococcus granulosus", Kirkuk Journal of Science, 10, 4, 2015, 119-133. doi: 10.32894/kujss.2015.124092
HARVARD
F. Hassan H, A.Saber J. (2015). 'Partial purification of cytidine deaminase from protoscoleces of Echinococcus granulosus', Kirkuk Journal of Science, 10(4), pp. 119-133. doi: 10.32894/kujss.2015.124092
CHICAGO
H F. Hassan and J A.Saber, "Partial purification of cytidine deaminase from protoscoleces of Echinococcus granulosus," Kirkuk Journal of Science, 10 4 (2015): 119-133, doi: 10.32894/kujss.2015.124092
VANCOUVER
F. Hassan H, A.Saber J. Partial purification of cytidine deaminase from protoscoleces of Echinococcus granulosus. Kirkuk J. Sci.. 2015;10(4):119-133. doi: 10.32894/kujss.2015.124092
