Purification of kidney alkaline phosphatase

Purification of kidney alkaline phosphatase.

Purification of Alkaline Phosphatase

8. An increase in the rate of progression of the bands down the column decreases the sharpness of the bands. On 'Zeo-Karb 215' (40-60 mesh/in.) a rate ofprogression of 10-15 cm./hr. gave satisfactory results. 9. Equations have been derived permitting the calculation ofthe proportion ofthe column occupied by a component, the width ofthe boundaries and the expected yield of pure components in sep...

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 and Partial Characterization of the Alkaline Phosphatase of Swine Kidney*

In 1957, we reported (1) the purification of alkaline phosphatase of swine kidney to a specific activity of about 150,000 units on a basis of total nitrogen content; the units were those as defined by Roche and Bouchilloux (2). At that time, this was the highest activity reported for any alkaline phosphatase, but one or two other workers have since appeared to achieve a similar order of activit...

Purification and properties of bovine synovial fluid alkaline phosphatase.

Alkaline phosphatase from bovine synovial fluid was purified 2300-fold. A molecular weight of 72,300 was determined from sucrose density gradient studies. The following monoesters were hydrolyzed by the enzyme: P-glycerophosphate, galactosamine 6-phosphate, glucosamice 6-phosphate, glucose 6-phosphate, o-phospho-L-serine, o-carboxyphenyl phosphate, phenyl phosphate, and p-nitrophenyl phosphate....