Affinity purified Pisum sativum lectin or agglutinin (PSA) is a heterodimer that consists of four subunits. It has a carbohydrate specificity towards α-linked mannose-containing oligosaccharides. It’s hemagglutinating activity can be inhibited by glucose, mannose, and sucrose. It does not have a blood group specificity. The N-terminal sequence of the lectin has shown some degree of homology compared to lectins from other legume species. Pisum sativum lectin has also shown mitogenic effect toward murine splenocytes and could inhibit activity of HIV-1 reverse transcriptase. PSA is often used to differentiate virally transformed from normal cells. Calcium and manganese ions are required for activity.
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Pisum sativum Lectin (PSA/PSL) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.