The purification of enolase from cerebral tissue

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Abstract
Enolase was ex-tracted with potassium chloride-EDTA solution from frozen ox brains; it was present in amounts averaging 13.2 [plus or minus] 1.8 units/g of tissue and represented 2.7 [plus or minus] 0.6% of the protein in the extract. A 35-fold purification was achieved and essentially pure enolase of specific activity 30 units/mg was obtained after chromatography on DEAE-Sephadex. The pure enzyme showed a marked tendency to undergo changes in its structure and state of aggregation, with an accompanying loss of activity. The effects on the enzyme reaction of temperature, magnesium concentration and compounds reacting with sulphydryl groups were investigated. The physical and chemical properties were very similar to those reported for enolase prepared from yeast or muscle.