Partial purification of adenosine deaminase from protoscoleces of Echinococcus granulosus

Abstract

Adenosine deaminase has been partially purified from protoscoleces of E. granulosus by gel filtration chromatography using Sephadex G100. The molecular weight of the enzyme determined by gel filtration was about 44000 dalton with specific activity about 920 nmole/ min/ mg protein and with purification fold of about 51. The optimum pH was found to be 7.2 at 37 o C with Km value of 0.028mM for adenosine. The results indicate that adenosine deaminase was extremely sensitive to inhibition by tubercidin, formycin A and cordycepin with inhibitory percentage of 82%, 86% and 78%, respectiv

Keywords

• purification
• adenosine deaminase
• protoscoleces
• echinococcus