The reversible inactivation of pig kidney alkaline phosphatase at low pH

Catalytic properties of alkaline phosphatase from pig kidney.

The enzymic properties of alkaline phosphatase (EC 3.1.3.1) from pig kidney brush-border membranes were studied. 1. It hydrolyses ortho- and pyro-phosphate esters, the rate limiting step (V(max.)) being independent of the substrate. It transphosphorylates to Tris at concentrations above 0.1m-Tris. 2. The pH optimum for hydrolysis was between 9.8 and 10. The pK of the enzyme-substrate complex is...

Bovine Kidney Alkaline Phosphatase

Kidney alkaline phosphatase was purified to homogeneity. It is a glycoprotein of about 172,000 molecular weight. Analyses of the subunit structure by sedimentation equilibrium in 6 M guanidine hydrochloride and by gel electrophoresis in sodium dodecyl sulfate indicate that the alkaline phosphatase is a dimer comprising two very similar or identical subunits of about 87,000 molecular weight. The...

Purification of kidney alkaline phosphatase.

Alkaline phosphatase activity and pH optima.

High pH values have been found necessary for optimum activity of alkaline phosphatase in vitro. The pH values in the living cell structures, on the other hand, are near neutrality: cytoplasm 6.9, nucleus 7.6 (l-3). This definite difference between the pH required for optimum activity and the pH of the living cell indicates that alkaline phosphatase is not optimally active in viva. However, the ...

Molecular aspects of the regulation of rat kidney alkaline phosphatase.

The mechanisms by which phosphate regulates the activity of alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) in rat kidney were investigated. Measurements of incorporation of [(14)C]leucine into kidney alkaline phosphatase in rats fed on complete or phosphate-free diet provide evidence of a twofold increase in the rate of synthesis of the enzyme in diet-treated anim...