Catalytic properties of alkaline phosphatase from pig kidney

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.

Purification and properties of alkaline phosphatase from rat chloroma.

Activity was determined by the rate of hydrolysis of 13-glycerophosphate on p-nitrophenyl phosphate (8). The determination with sodium 13-glycerophosphate was carried out as follows. The reaction mixture consisted of 0.05 M Tnis-HC1 (pH 10), 0.023 M sodium 13-glycerophosphate, 0.004 M MgCl2, and enzyme in a final volume of 2 ml. After incubation at 37° for 30 mm, 2 ml of 10% tnicbloroacetic ac...

The catalytic-centre activity and kinetic properties of bovine milk alkaline phosphatase.

1. The phosphorylation of milk alkaline phosphatase was studied under various conditions: maximum incorporation occurred at pH5.0 and 50% incorporation at pH6.6-7.0. 2. The phosphorylation was shown to be specific and the results suggest that the active centre of the enzyme is involved in the process. 3. Phosphoryl-enzyme is rapidly hydrolysed at alkaline pH. at pH7.0 the results suggest that a...