Adenosine triphosphate-creatine phosphotransferase from ox brain: purification and isolation

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Abstract
Adenosine triphosphate-creatine phosphotransferase was extracted with potassium chloride solution from ox brains; it was present in amounts averaging 24 [plus or minus]11 units/g of tissue and represented approx. 2% of the protein in the extract. A 50-fold purification was achieved and each step of the procedure was followed by cellulose acetate and starch-gel electrophoresis. The pure enzyme had a specific activity of 73 units/mg (component I). The enzyme was obtained in three peaks from a diethylaminoethyl-Sephadex column. Two of these peaks appeared to consist of interconvertible forms of the pure enzyme, whereas the third peak contained the enzyme in association with D-2-phosphoglycerate hydro-lyase and other foreign proteins. Marked activation was obtained with thiols, and the enzyme appeared to be less stable to heat, alcohols and storage than the corresponding enzyme from muscle.