Purification and characterization of a low-molecular-weight bovine kidney acid phosphatase.

@article{Granjeiro1997PurificationAC,
  title={Purification and characterization of a low-molecular-weight bovine kidney acid phosphatase.},
  author={Jos{\'e} Mauro Granjeiro and Eul{\'a}zio Mikio Taga and Hiroshi Aoyama},
  journal={Anais da Academia Brasileira de Ciencias},
  year={1997},
  volume={69 4},
  pages={451-60}
}
A relative low molecular mass bovine kidney acid phosphatase was purified 1,640-fold to homogeneity, with 7% recovery. The purified enzyme (specific activity 100 mumol min-1 mg-1) was electrophoretically homogeneous with a relative molecular mass of 17.8 kDa, as determined by SDS-polyacrylamide gel electrophoresis. A broad pH optimum of 4.0-5.5 and a maximal enzyme activity at 60 degrees C were determined for the p-nitrophenyl phosphate hydrolysis. Apparent Km values of 0.14 mM, 0.4 mM, 0.3 mM… CONTINUE READING

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