Human placental alkaline phosphatase: molecular weight and subunit structure.

@article{Gottlieb1968HumanPA,
  title={Human placental alkaline phosphatase: molecular weight and subunit structure.},
  author={Arlan J. Gottlieb and Howard H. Sussman},
  journal={Biochimica et biophysica acta},
  year={1968},
  volume={160 2},
  pages={
          167-71
        }
}
Abstract The molecular weight of human placental alkaline phosphatase and its subunits was investigated. The results were compared to those obtained with Escherichia coli alkaline phosphatase since its subunit structure has been well studied. These studies show that the placental enzyme like the E. Coli enzyme is a dimer. It has a mol. wt. of 116 000 and is composed of monomer subunits having an identical mol. wt. of 58 000. The E. coli phosphatase gave a mol. wt. of 90 500 for the native… CONTINUE READING

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