Some properties of 2,3-bisphosphoglycerate phosphatase from rabbit masseters.
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概要
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1. 2, 3-Bisphosphoglycerate phosphatase was partly purified by CM-cellulose column chromatography.<BR>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.<BR>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.<BR>4. The reaction mechanism was of a ping-pong type.<BR>5. Inhibition types of dihydroxyacetone phosphate and glyceraldehyde phosphate were uncompetitive against 2, 3-bisphosphoglycerate and competitive against 2-phosphoglycolate.
- 日本大学歯学部の論文
日本大学歯学部 | 論文
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