Abstract
A phytohemagglutinin has been isolated from seeds of Vicia faba L. var. minor, cv. “Dornburger Ackerbohne”, by means of affinity chromatography on dextran gels. This protein with a mol. wt. of about 48,500 D agglutinates human erythrocytes of all blood groups, and exhibits mitogenic activity with human lymphocytes. In the presence of 8 M urea the phytohemagglutinin dissociates into one type of heavy and one type of light subunit, which can be separated by gel filtration and ion exchange chromatography. From data of sodium dodecyl sulphate gel electrophoresis and amino acid composition mol. wts. of 18,800 D and 5,500 D are calculated for the heavy and the light sub-unit, respectively. A tetramer, consisting of two molecules each of heavy and light subunit, is proposed as quaternary structure of the phytohemagglutinin.
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