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

European Journal of Biochemistry
X GrañaF Climent

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.

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Citations

Jun 27, 2007·Biotechnology and Bioengineering·Christophe ChassagnoleMatthias Reuss
Oct 1, 1995·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·X GrañaF Climent
Aug 23, 2011·Biotechnology and Bioengineering·Angela CintolesiRamon Gonzalez
Jun 27, 2021·The Plant Journal : for Cell and Molecular Biology·Pauline DuminilNathalie Glab
Jan 21, 2011·Journal of Plant Physiology·Hedia TnaniCarlos M Vicient

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