Summary
β-Glycerophosphatase prepared from the intestinal mucosa of the calf was purified by fractionated precipitation with alcohol. A further concentration of the enzyme activity was attained by electrophoresis.
The activity of the purified enzyme solution was reduced to 1/5 of its original value when dialysed for 48 hours atp H 4.5. Atp H 6 and atp H 10.5 only a less pronounced decrease of the activity occurred.
By addition of heat-inactivatedβ-glycerophosphatase to the enzyme solution which was partly inactivated by dialysis atp H 4.5 the activity of the latter was increased by about 100%.
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v. Euler, H., Hahn, L. Aktivierung einer alkalischen Phosphatase. Experientia 3, 412–414 (1947). https://doi.org/10.1007/BF02156365
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DOI: https://doi.org/10.1007/BF02156365