Das Kreatin aufbauende Ferment des quergestreiften Muskels

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Abstract
The apoenzyme soln. was prepared by mincing the hind leg muscles of a frog, adding 2 cc. neutral phosphate buffer for 1 g. of the tissue in a centrifuge tube, and allowing the mixture to stand at 40[degree] for 1 hr. with frequent stirring. After centrifuging, the supernatant soln. was used for the expts. The cooking juice was obtained by boiling 5 g. of the minced muscle in 20 cc. phosphate buffer at pH 7.0 or in H2O. The filtrate obtained from this mixture was used. The reaction mixtures usually contained 2-4 cc. of the apoenzyme extract, 2 cc. of the cooking juice, 2-5 cc. phosphate buffer, 10-40 mg. of arginine and histidine HC1, 1 g. extracted muscle residue, etc. The reactions were carried out for 3 hrs. at 18[degree]. Neither the enzyme extract nor the extracted residue alone could synthesize creatine from arginine and histidine, while the combined extract and residue effected the synthesis. The cooking juice also activated the extract so that it brought about the synthesis. The insolubility of the apoenzyme in H2O and its solubility in salt solns. indicated its globulin nature. The muscle globulin myosine had the characteristics of the apoenzyme, and in the presence of the cooking juice, converted arginine and histidine into creatine. Myogen, globulin, X, serum albumin and globulin and fibrinogen were not active as apoenzymes.

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