Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum.

@article{Mccomb1972StudyOO,
  title={Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum.},
  author={R. Mccomb and G. Bowers},
  journal={Clinical chemistry},
  year={1972},
  volume={18 2},
  pages={
          97-104
        }
}
We have compared 23 compounds, with and without transphosphorylating properties, as buffer systems for human serum alkaline phosphatase activity, with p -nitrophenylphosphate as substrate. Relative enzyme activity in four representative buffers at near-optimal conditions was ethylaminoethanol > diethanolamine > 2-amino-2-methyl-1-propanol > carbonate. Transphosphorylation was demonstrated in the two buffers in which the enzyme was most active, ethylaminoethanol and diethanolamine. The optima… Expand
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