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. 1974 Jul;141(1):273-82.
doi: 10.1042/bj1410273.

Alkaline phosphatase from pig kidney. Method of purification and molecular properties

E D Wachsmuth, K Hiwada

Alkaline phosphatase from pig kidney. Method of purification and molecular properties

E D Wachsmuth et al. Biochem J. 1974 Jul.

Abstract

Alkaline phosphatase (EC 3.1.3.1) from pig kidney brush-border membranes was solubilized from membrane precipitates by butan-1-ol at a critical pH of 7.0. The 12000-fold purification procedure included (NH(4))(2)SO(4) precipitation, DEAE-and TEAE-cellulose chromatography, Sephadex G-200 gel filtration and neuraminidase digestion followed by DEAE-cellulose chromatography. The purified protein contained 20% (w/w) carbohydrate and had mol.wt. 150000-156000 as estimated by Sephadex filtration and ultracentrifuge analysis. It was a tetrameric glycoprotein consisting of identical subunits, and it had a molecular activity at 25 degrees C of 2600s(-1) per tetramer. Its concentration in kidney was estimated to be 8.5-8.8mg/kg.

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