PURIFICATION AND IMMUNOHISTOCHEMICAL STUDY OF ALKALINE PHOSPHATASE IN BOVINE KIDNEY

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 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....

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...

Isozymes of bovine intestinal alkaline phosphatase.

Alkaline phosphatases from calf and bovine small intestines have been isolated in homogeneous form from both mucosa and luminal contents. The detergent-solubilized calf enzyme resolves into two peaks of activity, C-1 and C-2, on chromatofocusing. Only one of these activity peaks is present in the enzyme from the adult animal. Amino acid compositions, N-terminal sequences, and tryptic peptide ma...