Large scale chromatographic purification of ribosome-in-activating proteins

A method for the purification of type 1 (single-chain) ribosome-inactivating proteins from large amounts of starting material has been developed. The general procedure can be adapted with minor modifications to the purification of a variety of such proteins either from seeds, saporins from Saponaria officinalis, momordin from Momordica charantia, trichokirin from Trichosanthes kirilowii, the protein from Hordeum vulgaris and gelonin from Gelonium multiflorum, or from leaves, dianthins from Dianthus caryophyllus. Yields ranged from 13 mg to 2.6 g of highly purified protein per kg of starting material. The amount of time and work was substantially reduced as compared with previously described procedures, and reusable gels have been employed during all chromatographic operations.