Abstract
Four proteolytic enzymes, euphorbains t1–t4, were isolated from the latex of the succulent Euphorbia tirucalli ("milk bush") and purified to homogeneity. The enzymes all have molecular weights of 74 000. Each enzyme has several different charged forms; t1, for example, has four with isoelectric points in the range of 5.0–5.5. The four proteases examined are of similar amino acid compositions but yield differing two-dimensional maps of tryptic digests. The euphorbain t's are not closely related in composition to their counterparts isolated from Euphorbia lathyris, Euphorbia pulcherrima, and Euphorbia cyparissias. The euphorbains from E. tirucalli were inhibited by phenylmethylsulphonyl fluoride and by histidine-specific reagents, and so are trypsin-like proteases.
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