Abstract
This chapter describes the isolation of prenyltransferase from human liver. Prenyltransferase has been purified to homogeneity from yeast, pig liver, and in crystalline form from chicken liver. The homogeneous human liver enzyme, the first sterol synthesizing enzyme to be purified from a human tissue, has properties distinct from the enzyme from these sources. Human liver prenyltransferase has an absolute requirement for divalent magnesium or manganese ions for activity. Not more than background activity is observed in the absence of divalent metals. This chapter highlights purification process of this enzyme. It consists of six steps namely—crude extract, ammonium sulfate fractionation, batch treatment with carboxymethyl cellulose, DEAE-cellulose column chromatography, butyl-agarose column chromatography, and calcium phosphate column chromatography.
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