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  • Title: Characterization of acid and alkaline phosphatase activity in preparations of tubulin and microtubule-associated proteins.
    Author: Prus K, Wallin M.
    Journal: FEBS Lett; 1983 Jan 10; 151(1):54-8. PubMed ID: 6825841.
    Abstract:
    Acid and alkaline phosphatase activity, determined by the hydrolysis of p-nitrophenyl phosphate, was found in preparations of microtubules purified from bovine brain by temperature-dependent assembly-disassembly and ion-exchange chromatography. Phosphocellulose-purified tubulin contained an associated acid phosphatase activity, stimulated by Mg2+ and by Zn2+. Alkaline phosphatase activity with a pH optimum of 10.4 was measured in a fraction of microtubule-associated proteins (MAPs). Kinetics and the effects of sodium fluoride, sodium tartrate, sulfhydryl-blocking agents, EDTA and Zn2+ are reported.
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