Purification, characterization and immunological properties of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize (Zea mays) seeds.
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.
Graña
X
X
Unitat de Bioquímica, Facultat de Medicina, Universitat de Barcelona, Spain.
Ureña
J
J
Ludevid
D
D
Carreras
J
J
Climent
F
F
D019794:2,3-Diphosphoglycerate; D000917:Antibody Formation; D001731:Bisphosphoglycerate Mutase / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D004163:Diphosphoglyceric Acids / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010770:Phosphotransferases / Q000302:isolation & purification*; D014176:Protein Biosynthesis; D012313:RNA / Q000302:isolation & purification; D003313:Zea mays / Q000201:enzymology*
D004163:Diphosphoglyceric Acids; D019794:2,3-Diphosphoglycerate; D012313:RNA; D010770:Phosphotransferases; D001731:Bisphosphoglycerate Mutase