A comparative study of the insoluble storage proteins and the lectins of seeds of the Euphorbiaceae

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Abstract
The major storage protein within seeds of the Euphorbiaceae is the 11S crystalloid, which is only completely soluble in buffer or salt solutions if sodium dodecylsulphate or urea is present. Prior to this study, only the storage proteins of the castor bean had been characterized. The nonreduced crystalloid protein complex in all species tested has a molecular weight of 50 000 – 55 000, and in reduced form the proteins migrate on polyacrylamide gels as two distinct groups of polypeptides, one in the molecular weight range 20 000 – 25 000 and the other in the 29 000 – 35 000 range. In this respect the proteins have the general characteristics of those of castor bean, but only the proteins of Jatropha gossypifolia show striking similarities. Within any one genus, the storage proteins appear to be more or less identical (e.g., Manihot spp.) or show distinct differences (e.g., Euphorbia spp.). The soluble lectin proteins of J. gossypifolia have very similar haemagglutination properties to those of castor bean lectins, and the glycoproteins of both species separate similarly on polyacrylamide gels. Few other species contain glycoproteins or lectins that can cause agglutination.