Abstract
In the rabbit and in the rat, which possess erythrocytes with high concentration of 2,3-bisphosphoglycerate, the 2,3-bisphosphoglycerate synthase activity increases more than two fold during reticulocyte maturation. Isolation of the enzymes with 2,3-bisphosphoglycerate synthase activity present in extracts of reticulocytes and mature erytrocytes by ion exchange fast liquid chromatography shows that the increase in the synthase activity is due to the accumulation of the bifunctional enzyme 2,3-bisphosphoglycerate synthase/phosphatase (EC 2.7.5.4/EC 3.1.3.13) which represents more than 80% of the synthase activity of the cell extracts. During reticulocyte maturation phosphoglycerate mutase (EC 5.4.2.1), which makes a small contribution to the 2,3-bisphosphoglycerate synthase activity in the erythroid cells, decreases in the rabbit and remains constant in the rat.
| Original language | English |
|---|---|
| Pages (from-to) | 183-188 |
| Number of pages | 6 |
| Journal | Molecular and Cellular Biochemistry |
| Volume | 102 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 1991 |
Keywords
- 2,3-bisphosphoglycerate synthase/phosphatase
- erythrocyte
- reticulocyte
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