1985 年 27 巻 3 号 p. 159-166
1. 2, 3-Bisphosphoglycerate phosphatase was partly purified by CM-cellulose column chromatography.
2. The enzyme activity was stable in the 50°C 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°C 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 phosphate were uncompetitive against 2, 3-bisphosphoglycerate and competitive against 2-phosphoglycolate.