Purification and properties of brain alkaline phosphatase

Dorai, D. Thambi ; Bachhawat, B. K. (1976) Purification and properties of brain alkaline phosphatase Journal of Neurochemistry, 29 (3). pp. 503-512. ISSN 0022-3042

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Official URL: http://www3.interscience.wiley.com/journal/1196275...

Related URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10699.x


Alkaline phosphatase from sheep brain has been purified to homogeneity. The method includes butanol extraction, fractional ethanol precipitation, ion-exchange chromatography on DEAE-cellulose, and on DEAE-Sephadex followed by Sephadex G-200 filtration. By these steps, the enzyme is purified 22,920-fold with 15% recovery. The homogeneous enzyme is shown to be a sialoglycoprotein in nature. Neuraminidase treatment reduces the electrophoretic mobility of the enzyme. The enzyme shows pyridoxal phosphate phosphatase activity along with p-nitrophenylphosphate phosphatase activity. Both these compounds behave as mutual alternate competitive substrates. The general properties of the enzyme are described.

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