Some properties of 2,3-bisphosphoglycerate phosphatase from rabbit masseters.

نویسندگان

  • M Maeno
  • M Ishida
  • K Otsuka
  • K Suzuki
چکیده

1. 2,3-Bisphosphoglycerate phosphatase was partly purified by CM-cellulose column chromatography. 2. The enzyme activity was stable in the 50•Ž case of preincubation up to 30 min. By the addition of 4 mM 2-phosphoglycolate to the preincubation mixture activity remained perfect up to 30 min in the 55•Ž case of preincubation. 3. This enzyme was inhibited by low concentrations of p-chloromercuribenzoate and heavy metal ions. These results suggest that this enzyme is an SH-enzyme. 4. The reaction mechanism was of a ping-pong type. 5. Inhibition types of dihydroxyacetone phosphate and glyceraldehyde phos-

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عنوان ژورنال:
  • The Journal of Nihon University School of Dentistry

دوره 27 3  شماره 

صفحات  -

تاریخ انتشار 1985