Purification, characterization and immunological properties of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize (Zea mays) seeds

Authors


Correspondence to F. Climent, Unitat de Bioquímica, Facultat de Medicina, Universitat de Barcelona, Casanova 143, E-08036 Barcelona, Spain

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.

Abbreviations
GriP mutase

phosphoglycerate mutase

Gri(2,3)P2

glycerate 2,3-bisphosphate

MTT

3-(4,5-dimethylthiazol-2yl)2,5-diphenyltetrazolium

Enzyme
 

Phosphoglycerate mutase (EC 5.4.2.1)