Non-toxic ribosome inactivating proteins (RIPs) with two chains,

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Plant proteins – e.g. – derived from legumes – algae or...

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435183, C07K 14415, A61K 3578

Patent

active

060083247

ABSTRACT:
The invention discloses ribosome inactivating proteins (RIPs) with two chains, which arc not toxic in the extra-cellular environment, of plant origin, and capable of interacting with ribonucleic acid and causing the inhibition of the biosynthesis of proteins in cellular systems, said proteins being comprised of two chains A and B, chain A having a N-glucosidase activity of the ribosomal ribonucleic acid, and chain B having a lectine activity, both chains being joined by disulphide bridges. Among the proteins, Nigrine b isolated from bark of Sambucus nigra L., basic Nigrine l isolated from the leaves of Sambucus nigra L., Ebuline 1 isolated from leaves of Sambucus ebulus L. and Racenosine b isolated from the bark of Sambucus racemosa L. are mentioned. The proteins find application as inactivators of the rebonucleic acid and as inhibitors of the protein synthesis.

REFERENCES:
patent: 4742046 (1988-05-01), Bliah
Biotechnology vol. 10, Apr. 1992 pp. 48 to 49.
Plant Molecular Biology, vol. 22, No. 6, Sep. 1993, "Isolation and Partial Characterization of Nigrin B. A Non-Toxic Novel Type 2 Ribosome-Inactivating Protein From The Bark of Sambucus nigra L." pp. 1181-1186.
Journal of Biological Chemistry, vol. 268, No. 24, Aug. 25, 1993, "Ebulin 1, A Nontoxic Novel Type 2 Ribosome-Inactivating Protein From Sambucus ebulus L.Leaves", pp. 18195-18199.

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