Immunoaffinity purification and comparison of allantoinases from soybean root nodules and cotyledons.

@article{Bell1995ImmunoaffinityPA,
  title={Immunoaffinity purification and comparison of allantoinases from soybean root nodules and cotyledons.},
  author={Jennifer A Bell and Mary Alice Webb},
  journal={Plant physiology},
  year={1995},
  volume={107 2},
  pages={435-41}
}
Allantoinase (allantoin amidohydrolase, EC 3.5.2.5) catalyzes the conversion of allantoin to allantoic acid in the final step of ureide biogenesis. We have purified allantoinase more than 4000-fold by immunoaffinity chromatography from root nodules and cotyledons of soybean (Glycine max [L] Merr.). We characterized and compared properties of the enzyme from the two sources. Seed and nodule allantoinases had 80% identity in the first 24 amino acid residues of the N terminus. Two-dimensional gel… CONTINUE READING