Summary
Alkaline phosphatase from tibia tendon ofMeleagris gallopavo L. was highly purified. The enzyme activation by different ions was measured. Mg2+ showed a high activation with a broader spectrum of phosphomonoester hydrolization. The in vivo Mg2+ concentration was an optimum for in vitro activation.
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Dedicated to Prof. Dr. G. Pfefferkorn on the occasion of his 65th birthday.
We thank Deutsche Forschungsgemeinschaft for support.
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Althoff, J., Quint, P. & Höhling, H.J. Activation and specificity of alkaline phosphatase of a mineralizing collagen-rich system. Experientia 34, 692–693 (1978). https://doi.org/10.1007/BF01947261
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DOI: https://doi.org/10.1007/BF01947261