Agglutinating activity

Human erythrocyte-agglutinating lectins were isolated from ethanol extracts of whole leaves of A. barbadensis and gel fillets of stabilized A. vera; from low- and high-speed supernatants of whole leaves of A. saponaria (Bouthet etal, 1996); from ethanol extracts of gel fillets of A. barbadensis; and, from whole leaves of A. arborescens (Aloctin A and Aloctin B) (Suzuki etal, 1979). Lectins isolated from whole leaves of A. saponaria also agglutinate canine erythrocytes (Winters etal., 1981) and Aloctins A and B also agglutinate sheep and rabbit erythrocytes (Suzuki etal., 1979).

Lectins isolated from the leaf gel of A. barbadensis (Aloctin I and Aloctin II) (Akev and Can, 1999) and a 35 kDa mannose-binding lection (Koike etal, 1995a) isolated from the leaf skin of A. arborescens agglutinate rabbit erythrocytes. Aloctins I and II also agglutinate rat erythrocytes (Akev and Can, 1999).

A 40 kDa lectin isolated from whole leaves of A. arborescens agglutinates sheep erythrocytes (Yagi etal, 1985), while ATF 1011 isolated from whole leaves of A. arborescens agglutinates tumor cells (Yoshimoto etal., 1987).

To our knowledge, A. barbadensis appears to have many lectins that agglutinate human erythrocytes.

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