Purification and properties of bovine synovial fluid alkaline phosphatase.

@article{Dabich1966PurificationAP,
  title={Purification and properties of bovine synovial fluid alkaline phosphatase.},
  author={Danica Dabich and O W Neuhaus},
  journal={The Journal of biological chemistry},
  year={1966},
  volume={241 2},
  pages={415-20}
}
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. Kinetic studies of the enzyme were made with p-nitrophenyl phosphate as substrate. Adenosine… CONTINUE READING