Characterization of heparinase from an oral bacterium Prevotella heparinolytica.

@article{Watanabe1998CharacterizationOH,
  title={Characterization of heparinase from an oral bacterium Prevotella heparinolytica.},
  author={Masahiko Watanabe and Hiroyuki Tsuda and Seiki Yamada and Yoshihiro Shibata and Takahiro J Nakamura and Kazuyuki Sugahara},
  journal={Journal of biochemistry},
  year={1998},
  volume={123 2},
  pages={
          283-8
        }
}
Heparinase was purified to homogeneity from the cell extract of an oral bacterium, Prevotella heparinolytica, by a combination of anion exchange chromatography, gel filtration chromatography, and hydroxyapatite chromatography. Properties of the purified P. heparinolytica heparinase (P. heparinase) were investigated. The enzyme exhibited a maximum activity in 50 mM Tris-HCl buffer, pH 7.5-8.0, containing 75 mM sodium acetate, 0.1 M NaCl, and 1 mM CaCl2. Optimum conditions for the maximum… CONTINUE READING

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