Abstract
The lectin from Solanum tuberosum is shown to be an inhibitor of invertase from the same plant. However, on the basis of pH curves and the dissociability of the respective complexes, a difference between lectin and proteinaceous inhibitors was established. This difference was confirmed by affinity chromatography on chitin columns. Kinetics of lectin inhibition is also described. Competition experiments between potato lectin and the proteinaceous inhibitor suggest that both substances are mutually exclusive. The proteinaceous inhibitor was also shown to agglutinate human erythrocytes.
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