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Preparation of highly purified momordin II without ribonuclease activity.

Momordin II, a ribosome-inactivating protein from Momordica charantia seeds, was purified by a procedure involving a series of chromatographies on S-Sepharose, Sephadex G-50, CM-Sepharose, and Red Sepharose columns. Highly purified momordin II inhibited cell-free protein synthesis, released adenine from rat liver ribosomes and from DNA, and had no RNase activity.[1]

References

  1. Preparation of highly purified momordin II without ribonuclease activity. Valbonesi, P., Barbieri, L., Bolognesi, A., Bonora, E., Polito, L., Stirpe, F. Life Sci. (1999) [Pubmed]
 
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