Cholinesterase from plasma of sheep was partially purified by ion exchange Chromatography on Phospho-Cellulose 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 Km value of2.7 x 1O·~ M Molecular weight of the enzyme was estimated to be approximately 400,000 daltons by gel filtration.
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