title: Purification and characterization of two lectins from Aloe arborescens Mill.
abstract: Two lectins have been isolated from leaves of Aloe arborescens Mill by salt precipitation, pH-dependent fractionation and gel filtration. One lectin (P-2) has a molecular weight of approximately 18,000, consists of two subunits (alphabeta) and contains more than 18% by weight of neutral carbohydrate. The smaller subunit (alpha) has a molecular weight of approximately 7,500 and the larger subunit (beta) a molecular weight of approximately 10,500. The other lectin (S-1) has a molecular weight of approximately 24,000, consists of two subunits (gamma2) with a molecular weight of approximately 12,000 and contains more than 50% by weight of neutral carbohydrate. An interesting feature of the amino acid compositions of these lectins is the high proportion of acidic amino acids, such as aspartic acid and glutamic acid, and the low proportion of methionine and histidine. S-1 has a strong hemagglutinating activity. On the other hand, P-2 has not only hemagglutinating activity but also mitogenic activity on lymphocytes, precipitate-forming reactivity with serum proteins, one of which is alpha2-macroglobulin, and complement C3 activating activity via the alternate pathway.
mesh_terms: D000504:Aloe / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001798:Blood Proteins; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D037102:Lectins / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D037121:Plant Lectins; D010946:Plants, Medicinal; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D001798:Blood Proteins; D037102:Lectins; D046911:Macromolecular Substances; D037121:Plant Lectins