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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530350, 530370, 4241951, A61K 3578, A61K 3700

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active

046720537

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.
Phytolaccin.sub.1 protein, purified according to the process of the invention, has been found to be an effective antiviral agent for the treatment of Herpes Simplex type II infections.

REFERENCES:
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