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Characterization of acid and alkaline phosphatase activity in preparations of tubulin and microtubule‐associated proteins
Author(s) -
Prus Karen,
Wallin Margareta
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80341-x
Subject(s) - tubulin , microtubule , alkaline phosphatase , biochemistry , chemistry , phosphatase , microbiology and biotechnology , biology , enzyme
Acid and alkaline phosphatase activity, determined by the hydrolysis of p ‐nitrophenyl phosphate, was found in preparation 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 Mg 2+ and Zn 2+ . 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 Zn 2+ are reported.