Properties of succinylated wheat-germ agglutinin.

@article{Monsigny1979PropertiesOS,
  title={Properties of succinylated wheat-germ agglutinin.},
  author={M. Monsigny and Christophe S{\'e}n{\'e} and A Obr{\'e}novitch and A. C. Roche and François Delmotte and Elisa Boschetti},
  journal={European journal of biochemistry},
  year={1979},
  volume={98 1},
  pages={39-45}
}
The physicochemical and binding properties of succinylated wheat germ agglutinin are described in comparison with these of unmodified wheat germ agglutinin. Succinylated wheat germ agglutinin is an acidic protein with a pI of 4.0 +/- 0.2 while the native lectin is basic, pI of 8.5. The solubility of succinylated wheat germ agglutinin is about 100 times higher than that of the unmodified lectin at neutral pH. Both lectins are dimeric at pH down to 5, and the dissociation occurs at pH lower than… CONTINUE READING

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