Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor.

@article{Hulett1986PurificationAC,
  title={Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor.},
  author={F. Marion Hulett and K V Stuckmann and Diana Spencer and T Sanopoulou},
  journal={Journal of general microbiology},
  year={1986},
  volume={132 8},
  pages={2387-95}
}
The most abundantly secreted protein from Bacillus licheniformis MC14 is alkaline phosphatase (APase). A twofold purification yields a homogeneous enzyme. No discernible chemical-physical differences in the secreted APase distinguish this enzyme from the cell-bound APase(s) except a 10-fold higher specific activity. During the growth phase in which the bacterium was secreting APase into the medium an inactive cytosol protein antigenically similar but 3000 Da heavier than the subunit of the… CONTINUE READING

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