A novel lectin was isolated from the leaf skin of "Kidachi Aloe" (Aloe arborescens Miller var. natalensis Berger) by sequential chromatographies on Sephadex G-25 gel filtration, DEAE ion exchange, and Superdex 75 gel filtration columns. The native lectin exhibited a molecular mass of about 35 kDa on both gel filtration on a Superdex 75 column and native-PAGE under nonreducing conditions. SDS-PAGE in the presence or absence of beta-mercaptoethanol revealed two distinct peptides with molecular masses of about 5.5 and 2.3 kDa, respectively, in addition to a major 9.2 kDa subunit, indicating the presence of a partially processed subunit. The N-terminal amino acid sequence of the intact subunit showed homology with that of snowdrop lectin. The native lectin showed hemagglutinating activity toward rabbit but not human and sheep erythrocytes, and specifically bound to mannose like snowdrop lectin did, indicating that the Aloe and snowdrop lectins are structurally and functionally similar proteins. In addition, the native lectin showed strong mitogenic activity toward mouse lymphocytes.