Kidney Phosphatase

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.

Phosphotransferase activities of kidney glucose 6-phosphatase.

Kidney glucose 6-phosphatase has been shown to catalyze inorganic pyrophosphatase and inorganic pyrophosphate-, cytidine diphosphate-, cytidine triphosphate-, and mannose 6-phosphate-glucose phosphotransferase reactions. The catalytic properties of phosphohydrolase and phosphotransferase activities of the kidney enzyme were found to be very similar to those of corresponding hepatic activities (...

The Disappearance of Phosphatase from the Hydronephrotic Kidney

"Alkaline" phosphatase disappears or only remains in small amounts in the rabbit and rat kidney after periods of hydronephrosis of 2 to 5 days or more, following complete obstruction of the ureter. By the use of the Gomori-Takamatsu technique it has been possible to distinguish normally functioning from non-functioning cells, when by ordinary histologic stains the cells are indistinguishable.

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...