Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum.

@article{Lam1998PurificationAC,
  title={Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum.},
  author={Stephanie S Lam and Hexiang Wang and T. B. Ng},
  journal={Biochemical and biophysical research communications},
  year={1998},
  volume={253 1},
  pages={135-42}
}
Two ribosome inactivating proteins designated alpha- and beta-pisavins were isolated from seeds of the garden pea Pisum sativum var. arvense Poir with a procedure involving affinity chromatography on Affi-gel Blue gel, immobilized metal ion affinity chromatography on Iminodiacetic acid-agarose, cation exchange chromatography on Resource-S, and gel filtration on Superose 12. alpha- and beta-pisavins are nonglycoproteins with a molecular weight of 20.5 kDa and 18.7 kDa respectively. The sequences… CONTINUE READING