Abstract
2,3‐Bisphosphoglycerate‐independent phosphoglycerate mutase (EC 5.4.2.1) was purified and characterized from maize. SDS electrophoresis showed only one band with a molecular mass of 64 kDa, similar to that determined for the native enzyme by gel‐filtration chromatography. The kinetic constants were similar to those reported for wheat germ phosphoglycerate mutase. Rabbit antiserum against maize phosphoglycerate mutase possesses a high degree of specificity. It also reacts with the wheat germ enzyme but fails to react with other cofactor‐independent or cofactor‐dependent phosphoglycerate mutases. Cell‐free synthesis experiments indicate that phosphoglycerate mutase from maize is not post‐translationally modified.
| Original language | English |
|---|---|
| Pages (from-to) | 149-153 |
| Number of pages | 5 |
| Journal | European Journal of Biochemistry |
| Volume | 186 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Dec 1989 |