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

Eur J Biochem. 1989 Dec 8;186(1-2):149-53. doi: 10.1111/j.1432-1033.1989.tb15189.x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2,3-Diphosphoglycerate
  • Antibody Formation
  • Bisphosphoglycerate Mutase / immunology
  • Bisphosphoglycerate Mutase / isolation & purification*
  • Bisphosphoglycerate Mutase / metabolism
  • Diphosphoglyceric Acids / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Phosphotransferases / isolation & purification*
  • Protein Biosynthesis
  • RNA / isolation & purification
  • Zea mays / enzymology*

Substances

  • Diphosphoglyceric Acids
  • 2,3-Diphosphoglycerate
  • RNA
  • Phosphotransferases
  • Bisphosphoglycerate Mutase