Abstract
Cholinesterase from plasma of sheep was partially purified by ion exchange Chromatography on Phospho-Celiulose column, gel filtration on Sepharose-6B and finally by affinity chromatography on Sepharose Con-A. The enzyme was purified 100 fold with specific activity of 440 mU/mg of protein with recovery of about 20%. The enzyme was found to be glycoprotein with Kin value of 2.7 x 10(M)(-5) Molecular weight of the enzyme was estimated to be approximately 400,000 daltons by gel filtration.