Immunoaffinity purification of phytolaccin proteins and their us

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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514 2, 530370, 530412, 530413, 424 941, A61K 3748, A61K 3700

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active

049218417

ABSTRACT:
Antiviral proteins phytolaccin.sub.1 and phytolaccin.sub.2 were isolated from the higher plant Phytolaccin americana using the technique of immunoaffinity chromatography. Phytolaccin proteins were purified to apparent homogeneity in a rapid and efficient chromatographic procedure utilizing immobilized monospecific anti-phytolaccin antibodies. Immunoaffinity-purified phytolaccin.sub.1 and phytolaccin.sub.2 were determined by denaturing gel electrophoresis to be of approximately 25,600 and 28,400 daltons, respectively. The two immunoaffinity-purified proteins were equally potent inhibitors of eukaryotic cell-free protein biosynthesis and exhibited mostly similar high-order UV derivative spectra. Antibodies against phytolaccin.sub.1 and phytolaccin.sub.2 did not cross-react with the heterologous antigen, indicating a structural dissimilarity between the two phytolaccin proteins.

REFERENCES:
patent: 4341761 (1982-07-01), Garfield et al.
Irvin, J.D., Arch Biochem Biophys, vol. 169, pp. 522-528, 1975, "Purification and Partial Characterization of the Antiviral Protein from Phytolacca americana which inhibits Eukaryotic Protein Synthesis".
Irvin et al., Arch Biochem Biophys, vol. 200 (2), pp. 418-425, 1980, "Purification and Properties of a Second Antiviral Protein from Phytolacca americana which Inactivates Eukaryotic Ribosomes.sup.1 ".
Barbieri et al., Biochem J, vol. 203, pp. 55-59, 1982, "Purification and Partial Characterization of another form of the Activiral Protein from the Sedds of Phytolacca americana L.(epokeweed)".
Orbig et al., Arch Biochem Biophys, vol. 155, pp. 278-287, 1973, "The Effect of an Antiviral Peptide on the Ribosonal Reactions of the Peptide Elongation Enzymes, EF-I and EF-II".

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